Structure and dynamics of the membrane attaching nitric oxide transporter nitrophorin 7 [v2; ref status: indexed, http://f1000r.es/5p1]

Nitrophorins represent a unique class of heme proteins that are able to perform the delicate transportation and release of the free-radical gaseous messenger nitric oxide (NO) in a pH-triggered manner. Besides its ability to bind to phospholipid membranes, the N-terminus of NP7, a member of the NO t...
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Autor*in:	Markus Knipp [verfasserIn] Hideaki Ogata [verfasserIn] Giancarlo Soavi [verfasserIn] Giulio Cerullo [verfasserIn] Alessandro Allegri [verfasserIn] Stefania Abbruzzetti [verfasserIn] Stefano Bruno [verfasserIn] Cristiano Viappiani [verfasserIn] Axel Bidon-Chanal [verfasserIn] F. Javier Luque [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2015

Schlagwörter:	Biomacromolecule-Ligand Interactions Chemical Biology of the Cell

Übergeordnetes Werk:	In: F1000Research - F1000 Research Ltd, 2013, 4(2015)
Übergeordnetes Werk:	volume:4 ; year:2015

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.12688/f1000research.6060.2

Katalog-ID:	DOAJ045183597

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allfields	10.12688/f1000research.6060.2 doi (DE-627)DOAJ045183597 (DE-599)DOAJbe667b434bde49d5ae46217204023218 DE-627 ger DE-627 rakwb eng Markus Knipp verfasserin aut Structure and dynamics of the membrane attaching nitric oxide transporter nitrophorin 7 [v2; ref status: indexed, http://f1000r.es/5p1] 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Nitrophorins represent a unique class of heme proteins that are able to perform the delicate transportation and release of the free-radical gaseous messenger nitric oxide (NO) in a pH-triggered manner. Besides its ability to bind to phospholipid membranes, the N-terminus of NP7, a member of the NO transporter nitrophorin family, contains an additional Leu-Pro-Gly stretch, which is a unique sequence trait, and the heme cavity is significantly altered with respect to other nitrophorins. These distinctive features encouraged us to solve the X-ray crystallographic structures of NP7 at low and high pH and bound with different heme ligands (nitric oxide, histamine, imidazole). The overall fold of the lipocalin motif is well preserved in the different X-ray structures and resembles the fold of other nitrophorins. However, a chain-like arrangement in the crystal lattice due to a number of head-to-tail electrostatic stabilizing interactions is found in NP7. Furthermore, the X-ray structures also reveal ligand-dependent changes in the orientation of the heme, as well as in specific interactions between the A-B and G-H loops, which are considered to be relevant for the biological function of nitrophorins. Fast and ultrafast laser triggered ligand rebinding experiments demonstrate the pH-dependent ligand migration within the cavities and the exit route. Finally, the topological distribution of pockets located around the heme as well as from inner cavities present at the rear of the protein provides a distinctive feature in NP7, so that while a loop gated exit mechanism to the solvent has been proposed for most nitrophorins, a more complex mechanism that involves several interconnected gas hosting cavities is proposed for NP7. Biomacromolecule-Ligand Interactions Chemical Biology of the Cell Medicine R Science Q Hideaki Ogata verfasserin aut Giancarlo Soavi verfasserin aut Giulio Cerullo verfasserin aut Alessandro Allegri verfasserin aut Stefania Abbruzzetti verfasserin aut Stefano Bruno verfasserin aut Cristiano Viappiani verfasserin aut Axel Bidon-Chanal verfasserin aut F. Javier Luque verfasserin aut In F1000Research F1000 Research Ltd, 2013 4(2015) (DE-627)735133581 (DE-600)2699932-8 20461402 nnns volume:4 year:2015 https://doi.org/10.12688/f1000research.6060.2 kostenfrei https://doaj.org/article/be667b434bde49d5ae46217204023218 kostenfrei http://f1000research.com/articles/4-45/v2 kostenfrei https://doaj.org/toc/2046-1402 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 2015
spelling	10.12688/f1000research.6060.2 doi (DE-627)DOAJ045183597 (DE-599)DOAJbe667b434bde49d5ae46217204023218 DE-627 ger DE-627 rakwb eng Markus Knipp verfasserin aut Structure and dynamics of the membrane attaching nitric oxide transporter nitrophorin 7 [v2; ref status: indexed, http://f1000r.es/5p1] 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Nitrophorins represent a unique class of heme proteins that are able to perform the delicate transportation and release of the free-radical gaseous messenger nitric oxide (NO) in a pH-triggered manner. Besides its ability to bind to phospholipid membranes, the N-terminus of NP7, a member of the NO transporter nitrophorin family, contains an additional Leu-Pro-Gly stretch, which is a unique sequence trait, and the heme cavity is significantly altered with respect to other nitrophorins. These distinctive features encouraged us to solve the X-ray crystallographic structures of NP7 at low and high pH and bound with different heme ligands (nitric oxide, histamine, imidazole). The overall fold of the lipocalin motif is well preserved in the different X-ray structures and resembles the fold of other nitrophorins. However, a chain-like arrangement in the crystal lattice due to a number of head-to-tail electrostatic stabilizing interactions is found in NP7. Furthermore, the X-ray structures also reveal ligand-dependent changes in the orientation of the heme, as well as in specific interactions between the A-B and G-H loops, which are considered to be relevant for the biological function of nitrophorins. Fast and ultrafast laser triggered ligand rebinding experiments demonstrate the pH-dependent ligand migration within the cavities and the exit route. Finally, the topological distribution of pockets located around the heme as well as from inner cavities present at the rear of the protein provides a distinctive feature in NP7, so that while a loop gated exit mechanism to the solvent has been proposed for most nitrophorins, a more complex mechanism that involves several interconnected gas hosting cavities is proposed for NP7. Biomacromolecule-Ligand Interactions Chemical Biology of the Cell Medicine R Science Q Hideaki Ogata verfasserin aut Giancarlo Soavi verfasserin aut Giulio Cerullo verfasserin aut Alessandro Allegri verfasserin aut Stefania Abbruzzetti verfasserin aut Stefano Bruno verfasserin aut Cristiano Viappiani verfasserin aut Axel Bidon-Chanal verfasserin aut F. Javier Luque verfasserin aut In F1000Research F1000 Research Ltd, 2013 4(2015) (DE-627)735133581 (DE-600)2699932-8 20461402 nnns volume:4 year:2015 https://doi.org/10.12688/f1000research.6060.2 kostenfrei https://doaj.org/article/be667b434bde49d5ae46217204023218 kostenfrei http://f1000research.com/articles/4-45/v2 kostenfrei https://doaj.org/toc/2046-1402 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 2015
allfields_unstemmed	10.12688/f1000research.6060.2 doi (DE-627)DOAJ045183597 (DE-599)DOAJbe667b434bde49d5ae46217204023218 DE-627 ger DE-627 rakwb eng Markus Knipp verfasserin aut Structure and dynamics of the membrane attaching nitric oxide transporter nitrophorin 7 [v2; ref status: indexed, http://f1000r.es/5p1] 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Nitrophorins represent a unique class of heme proteins that are able to perform the delicate transportation and release of the free-radical gaseous messenger nitric oxide (NO) in a pH-triggered manner. Besides its ability to bind to phospholipid membranes, the N-terminus of NP7, a member of the NO transporter nitrophorin family, contains an additional Leu-Pro-Gly stretch, which is a unique sequence trait, and the heme cavity is significantly altered with respect to other nitrophorins. These distinctive features encouraged us to solve the X-ray crystallographic structures of NP7 at low and high pH and bound with different heme ligands (nitric oxide, histamine, imidazole). The overall fold of the lipocalin motif is well preserved in the different X-ray structures and resembles the fold of other nitrophorins. However, a chain-like arrangement in the crystal lattice due to a number of head-to-tail electrostatic stabilizing interactions is found in NP7. Furthermore, the X-ray structures also reveal ligand-dependent changes in the orientation of the heme, as well as in specific interactions between the A-B and G-H loops, which are considered to be relevant for the biological function of nitrophorins. Fast and ultrafast laser triggered ligand rebinding experiments demonstrate the pH-dependent ligand migration within the cavities and the exit route. Finally, the topological distribution of pockets located around the heme as well as from inner cavities present at the rear of the protein provides a distinctive feature in NP7, so that while a loop gated exit mechanism to the solvent has been proposed for most nitrophorins, a more complex mechanism that involves several interconnected gas hosting cavities is proposed for NP7. Biomacromolecule-Ligand Interactions Chemical Biology of the Cell Medicine R Science Q Hideaki Ogata verfasserin aut Giancarlo Soavi verfasserin aut Giulio Cerullo verfasserin aut Alessandro Allegri verfasserin aut Stefania Abbruzzetti verfasserin aut Stefano Bruno verfasserin aut Cristiano Viappiani verfasserin aut Axel Bidon-Chanal verfasserin aut F. Javier Luque verfasserin aut In F1000Research F1000 Research Ltd, 2013 4(2015) (DE-627)735133581 (DE-600)2699932-8 20461402 nnns volume:4 year:2015 https://doi.org/10.12688/f1000research.6060.2 kostenfrei https://doaj.org/article/be667b434bde49d5ae46217204023218 kostenfrei http://f1000research.com/articles/4-45/v2 kostenfrei https://doaj.org/toc/2046-1402 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 2015
allfieldsGer	10.12688/f1000research.6060.2 doi (DE-627)DOAJ045183597 (DE-599)DOAJbe667b434bde49d5ae46217204023218 DE-627 ger DE-627 rakwb eng Markus Knipp verfasserin aut Structure and dynamics of the membrane attaching nitric oxide transporter nitrophorin 7 [v2; ref status: indexed, http://f1000r.es/5p1] 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Nitrophorins represent a unique class of heme proteins that are able to perform the delicate transportation and release of the free-radical gaseous messenger nitric oxide (NO) in a pH-triggered manner. Besides its ability to bind to phospholipid membranes, the N-terminus of NP7, a member of the NO transporter nitrophorin family, contains an additional Leu-Pro-Gly stretch, which is a unique sequence trait, and the heme cavity is significantly altered with respect to other nitrophorins. These distinctive features encouraged us to solve the X-ray crystallographic structures of NP7 at low and high pH and bound with different heme ligands (nitric oxide, histamine, imidazole). The overall fold of the lipocalin motif is well preserved in the different X-ray structures and resembles the fold of other nitrophorins. However, a chain-like arrangement in the crystal lattice due to a number of head-to-tail electrostatic stabilizing interactions is found in NP7. Furthermore, the X-ray structures also reveal ligand-dependent changes in the orientation of the heme, as well as in specific interactions between the A-B and G-H loops, which are considered to be relevant for the biological function of nitrophorins. Fast and ultrafast laser triggered ligand rebinding experiments demonstrate the pH-dependent ligand migration within the cavities and the exit route. Finally, the topological distribution of pockets located around the heme as well as from inner cavities present at the rear of the protein provides a distinctive feature in NP7, so that while a loop gated exit mechanism to the solvent has been proposed for most nitrophorins, a more complex mechanism that involves several interconnected gas hosting cavities is proposed for NP7. Biomacromolecule-Ligand Interactions Chemical Biology of the Cell Medicine R Science Q Hideaki Ogata verfasserin aut Giancarlo Soavi verfasserin aut Giulio Cerullo verfasserin aut Alessandro Allegri verfasserin aut Stefania Abbruzzetti verfasserin aut Stefano Bruno verfasserin aut Cristiano Viappiani verfasserin aut Axel Bidon-Chanal verfasserin aut F. Javier Luque verfasserin aut In F1000Research F1000 Research Ltd, 2013 4(2015) (DE-627)735133581 (DE-600)2699932-8 20461402 nnns volume:4 year:2015 https://doi.org/10.12688/f1000research.6060.2 kostenfrei https://doaj.org/article/be667b434bde49d5ae46217204023218 kostenfrei http://f1000research.com/articles/4-45/v2 kostenfrei https://doaj.org/toc/2046-1402 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 2015
allfieldsSound	10.12688/f1000research.6060.2 doi (DE-627)DOAJ045183597 (DE-599)DOAJbe667b434bde49d5ae46217204023218 DE-627 ger DE-627 rakwb eng Markus Knipp verfasserin aut Structure and dynamics of the membrane attaching nitric oxide transporter nitrophorin 7 [v2; ref status: indexed, http://f1000r.es/5p1] 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Nitrophorins represent a unique class of heme proteins that are able to perform the delicate transportation and release of the free-radical gaseous messenger nitric oxide (NO) in a pH-triggered manner. Besides its ability to bind to phospholipid membranes, the N-terminus of NP7, a member of the NO transporter nitrophorin family, contains an additional Leu-Pro-Gly stretch, which is a unique sequence trait, and the heme cavity is significantly altered with respect to other nitrophorins. These distinctive features encouraged us to solve the X-ray crystallographic structures of NP7 at low and high pH and bound with different heme ligands (nitric oxide, histamine, imidazole). The overall fold of the lipocalin motif is well preserved in the different X-ray structures and resembles the fold of other nitrophorins. However, a chain-like arrangement in the crystal lattice due to a number of head-to-tail electrostatic stabilizing interactions is found in NP7. Furthermore, the X-ray structures also reveal ligand-dependent changes in the orientation of the heme, as well as in specific interactions between the A-B and G-H loops, which are considered to be relevant for the biological function of nitrophorins. Fast and ultrafast laser triggered ligand rebinding experiments demonstrate the pH-dependent ligand migration within the cavities and the exit route. Finally, the topological distribution of pockets located around the heme as well as from inner cavities present at the rear of the protein provides a distinctive feature in NP7, so that while a loop gated exit mechanism to the solvent has been proposed for most nitrophorins, a more complex mechanism that involves several interconnected gas hosting cavities is proposed for NP7. Biomacromolecule-Ligand Interactions Chemical Biology of the Cell Medicine R Science Q Hideaki Ogata verfasserin aut Giancarlo Soavi verfasserin aut Giulio Cerullo verfasserin aut Alessandro Allegri verfasserin aut Stefania Abbruzzetti verfasserin aut Stefano Bruno verfasserin aut Cristiano Viappiani verfasserin aut Axel Bidon-Chanal verfasserin aut F. Javier Luque verfasserin aut In F1000Research F1000 Research Ltd, 2013 4(2015) (DE-627)735133581 (DE-600)2699932-8 20461402 nnns volume:4 year:2015 https://doi.org/10.12688/f1000research.6060.2 kostenfrei https://doaj.org/article/be667b434bde49d5ae46217204023218 kostenfrei http://f1000research.com/articles/4-45/v2 kostenfrei https://doaj.org/toc/2046-1402 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 4 2015
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author	Markus Knipp
spellingShingle	Markus Knipp misc Biomacromolecule-Ligand Interactions misc Chemical Biology of the Cell misc Medicine misc R misc Science misc Q Structure and dynamics of the membrane attaching nitric oxide transporter nitrophorin 7 [v2; ref status: indexed, http://f1000r.es/5p1]
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topic_title	Structure and dynamics of the membrane attaching nitric oxide transporter nitrophorin 7 [v2; ref status: indexed, http://f1000r.es/5p1] Biomacromolecule-Ligand Interactions Chemical Biology of the Cell
topic	misc Biomacromolecule-Ligand Interactions misc Chemical Biology of the Cell misc Medicine misc R misc Science misc Q
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title	Structure and dynamics of the membrane attaching nitric oxide transporter nitrophorin 7 [v2; ref status: indexed, http://f1000r.es/5p1]
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title_full	Structure and dynamics of the membrane attaching nitric oxide transporter nitrophorin 7 [v2; ref status: indexed, http://f1000r.es/5p1]
author_sort	Markus Knipp
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author_browse	Markus Knipp Hideaki Ogata Giancarlo Soavi Giulio Cerullo Alessandro Allegri Stefania Abbruzzetti Stefano Bruno Cristiano Viappiani Axel Bidon-Chanal F. Javier Luque
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title_sort	structure and dynamics of the membrane attaching nitric oxide transporter nitrophorin 7 [v2; ref status: indexed, http://f1000r.es/5p1]
title_auth	Structure and dynamics of the membrane attaching nitric oxide transporter nitrophorin 7 [v2; ref status: indexed, http://f1000r.es/5p1]
abstract	Nitrophorins represent a unique class of heme proteins that are able to perform the delicate transportation and release of the free-radical gaseous messenger nitric oxide (NO) in a pH-triggered manner. Besides its ability to bind to phospholipid membranes, the N-terminus of NP7, a member of the NO transporter nitrophorin family, contains an additional Leu-Pro-Gly stretch, which is a unique sequence trait, and the heme cavity is significantly altered with respect to other nitrophorins. These distinctive features encouraged us to solve the X-ray crystallographic structures of NP7 at low and high pH and bound with different heme ligands (nitric oxide, histamine, imidazole). The overall fold of the lipocalin motif is well preserved in the different X-ray structures and resembles the fold of other nitrophorins. However, a chain-like arrangement in the crystal lattice due to a number of head-to-tail electrostatic stabilizing interactions is found in NP7. Furthermore, the X-ray structures also reveal ligand-dependent changes in the orientation of the heme, as well as in specific interactions between the A-B and G-H loops, which are considered to be relevant for the biological function of nitrophorins. Fast and ultrafast laser triggered ligand rebinding experiments demonstrate the pH-dependent ligand migration within the cavities and the exit route. Finally, the topological distribution of pockets located around the heme as well as from inner cavities present at the rear of the protein provides a distinctive feature in NP7, so that while a loop gated exit mechanism to the solvent has been proposed for most nitrophorins, a more complex mechanism that involves several interconnected gas hosting cavities is proposed for NP7.
abstractGer	Nitrophorins represent a unique class of heme proteins that are able to perform the delicate transportation and release of the free-radical gaseous messenger nitric oxide (NO) in a pH-triggered manner. Besides its ability to bind to phospholipid membranes, the N-terminus of NP7, a member of the NO transporter nitrophorin family, contains an additional Leu-Pro-Gly stretch, which is a unique sequence trait, and the heme cavity is significantly altered with respect to other nitrophorins. These distinctive features encouraged us to solve the X-ray crystallographic structures of NP7 at low and high pH and bound with different heme ligands (nitric oxide, histamine, imidazole). The overall fold of the lipocalin motif is well preserved in the different X-ray structures and resembles the fold of other nitrophorins. However, a chain-like arrangement in the crystal lattice due to a number of head-to-tail electrostatic stabilizing interactions is found in NP7. Furthermore, the X-ray structures also reveal ligand-dependent changes in the orientation of the heme, as well as in specific interactions between the A-B and G-H loops, which are considered to be relevant for the biological function of nitrophorins. Fast and ultrafast laser triggered ligand rebinding experiments demonstrate the pH-dependent ligand migration within the cavities and the exit route. Finally, the topological distribution of pockets located around the heme as well as from inner cavities present at the rear of the protein provides a distinctive feature in NP7, so that while a loop gated exit mechanism to the solvent has been proposed for most nitrophorins, a more complex mechanism that involves several interconnected gas hosting cavities is proposed for NP7.
abstract_unstemmed	Nitrophorins represent a unique class of heme proteins that are able to perform the delicate transportation and release of the free-radical gaseous messenger nitric oxide (NO) in a pH-triggered manner. Besides its ability to bind to phospholipid membranes, the N-terminus of NP7, a member of the NO transporter nitrophorin family, contains an additional Leu-Pro-Gly stretch, which is a unique sequence trait, and the heme cavity is significantly altered with respect to other nitrophorins. These distinctive features encouraged us to solve the X-ray crystallographic structures of NP7 at low and high pH and bound with different heme ligands (nitric oxide, histamine, imidazole). The overall fold of the lipocalin motif is well preserved in the different X-ray structures and resembles the fold of other nitrophorins. However, a chain-like arrangement in the crystal lattice due to a number of head-to-tail electrostatic stabilizing interactions is found in NP7. Furthermore, the X-ray structures also reveal ligand-dependent changes in the orientation of the heme, as well as in specific interactions between the A-B and G-H loops, which are considered to be relevant for the biological function of nitrophorins. Fast and ultrafast laser triggered ligand rebinding experiments demonstrate the pH-dependent ligand migration within the cavities and the exit route. Finally, the topological distribution of pockets located around the heme as well as from inner cavities present at the rear of the protein provides a distinctive feature in NP7, so that while a loop gated exit mechanism to the solvent has been proposed for most nitrophorins, a more complex mechanism that involves several interconnected gas hosting cavities is proposed for NP7.
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title_short	Structure and dynamics of the membrane attaching nitric oxide transporter nitrophorin 7 [v2; ref status: indexed, http://f1000r.es/5p1]
url	https://doi.org/10.12688/f1000research.6060.2 https://doaj.org/article/be667b434bde49d5ae46217204023218 http://f1000research.com/articles/4-45/v2 https://doaj.org/toc/2046-1402
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up_date	2024-07-03T13:28:59.126Z
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Besides its ability to bind to phospholipid membranes, the N-terminus of NP7, a member of the NO transporter nitrophorin family, contains an additional Leu-Pro-Gly stretch, which is a unique sequence trait, and the heme cavity is significantly altered with respect to other nitrophorins. These distinctive features encouraged us to solve the X-ray crystallographic structures of NP7 at low and high pH and bound with different heme ligands (nitric oxide, histamine, imidazole). The overall fold of the lipocalin motif is well preserved in the different X-ray structures and resembles the fold of other nitrophorins. However, a chain-like arrangement in the crystal lattice due to a number of head-to-tail electrostatic stabilizing interactions is found in NP7. 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