De novo phasing with X-ray laser reveals mosquito larvicide BinAB structure
BinAB is a naturally occurring paracrystalline larvicide distributed worldwide to combat the devastating diseases borne by mosquitoes. These crystals are composed of homologous molecules, BinA and BinB, which play distinct roles in the multi-step intoxication process, transforming from harmless, rob...
Ausführliche Beschreibung
Autor*in: |
Jacques-Philippe Colletier [verfasserIn] |
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Format: |
Artikel |
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Sprache: |
Englisch |
Erschienen: |
2016 |
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Schlagwörter: |
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Übergeordnetes Werk: |
Enthalten in: Nature - London : Macmillan Publishers Limited, part of Springer Nature, 1869, 539(2016), 7627, Seite 43-47 |
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Übergeordnetes Werk: |
volume:539 ; year:2016 ; number:7627 ; pages:43-47 |
Links: |
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DOI / URN: |
10.1038/nature19825 |
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Katalog-ID: |
OLC1984925571 |
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520 | |a BinAB is a naturally occurring paracrystalline larvicide distributed worldwide to combat the devastating diseases borne by mosquitoes. These crystals are composed of homologous molecules, BinA and BinB, which play distinct roles in the multi-step intoxication process, transforming from harmless, robust crystals, to soluble protoxin heterodimers, to internalized mature toxin, and finally to toxic oligomeric pores. The small size of the crystals-50 unit cells per edge, on average-has impeded structural characterization by conventional means. Here we report the structure of Lysinibacillus sphaericus BinAB solved de novo by serial-femtosecond crystallography at an X-ray free-electron laser. The structure reveals tyrosine- and carboxylate-mediated contacts acting as pH switches to release soluble protoxin in the alkaline larval midgut. An enormous heterodimeric interface appears to be responsible for anchoring BinA to receptor-bound BinB for co-internalization. Remarkably, this interface is largely composed of propeptides, suggesting that proteolytic maturation would trigger dissociation of the heterodimer and progression to pore formation. | ||
650 | 4 | |a Mosquitoes | |
650 | 4 | |a Crystals | |
650 | 4 | |a Toxicity | |
650 | 4 | |a Pesticides | |
650 | 4 | |a X-ray lasers | |
650 | 4 | |a Pesticide residues | |
650 | 4 | |a Health aspects | |
650 | 4 | |a Structure | |
650 | 4 | |a Observations | |
650 | 4 | |a Usage | |
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700 | 0 | |a Mari Gingery |4 oth | |
700 | 0 | |a Jose A Rodriguez |4 oth | |
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700 | 0 | |a Daniel P DePonte |4 oth | |
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700 | 0 | |a Mark S Hunter |4 oth | |
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700 | 0 | |a Dennis K Bideshi |4 oth | |
700 | 0 | |a Axel T Brunger |4 oth | |
700 | 0 | |a Brian A Federici |4 oth | |
700 | 0 | |a Nicholas K Sauter |4 oth | |
700 | 0 | |a David S Eisenberg |4 oth | |
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10.1038/nature19825 doi PQ20170301 (DE-627)OLC1984925571 (DE-599)GBVOLC1984925571 (PRQ)c1825-7e411c36e881f0b8b2a3717ea97fe975e7836bf8622b35cffa367683ab5a78c80 (KEY)0072945020160000539762700043novophasingwithxraylaserrevealsmosquitolarvicidebi DE-627 ger DE-627 rakwb eng 070 500 DE-101 500 AVZ BIODIV fid Jacques-Philippe Colletier verfasserin aut De novo phasing with X-ray laser reveals mosquito larvicide BinAB structure 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier BinAB is a naturally occurring paracrystalline larvicide distributed worldwide to combat the devastating diseases borne by mosquitoes. These crystals are composed of homologous molecules, BinA and BinB, which play distinct roles in the multi-step intoxication process, transforming from harmless, robust crystals, to soluble protoxin heterodimers, to internalized mature toxin, and finally to toxic oligomeric pores. The small size of the crystals-50 unit cells per edge, on average-has impeded structural characterization by conventional means. Here we report the structure of Lysinibacillus sphaericus BinAB solved de novo by serial-femtosecond crystallography at an X-ray free-electron laser. The structure reveals tyrosine- and carboxylate-mediated contacts acting as pH switches to release soluble protoxin in the alkaline larval midgut. An enormous heterodimeric interface appears to be responsible for anchoring BinA to receptor-bound BinB for co-internalization. Remarkably, this interface is largely composed of propeptides, suggesting that proteolytic maturation would trigger dissociation of the heterodimer and progression to pore formation. Mosquitoes Crystals Toxicity Pesticides X-ray lasers Pesticide residues Health aspects Structure Observations Usage Michael R Sawaya oth Mari Gingery oth Jose A Rodriguez oth Duilio Cascio oth Aaron S Brewster oth Tara Michels-Clark oth Robert H Hice oth Nicolas Coquelle oth Sébastien Boutet oth Garth J Williams oth Marc Messerschmidt oth Daniel P DePonte oth Raymond G Sierra oth Hartawan Laksmono oth Jason E Koglin oth Mark S Hunter oth Hyun-Woo Park oth Monarin Uervirojnangkoorn oth Dennis K Bideshi oth Axel T Brunger oth Brian A Federici oth Nicholas K Sauter oth David S Eisenberg oth Enthalten in Nature London : Macmillan Publishers Limited, part of Springer Nature, 1869 539(2016), 7627, Seite 43-47 (DE-627)129292834 (DE-600)120714-3 (DE-576)014473941 0028-0836 nnns volume:539 year:2016 number:7627 pages:43-47 http://dx.doi.org/10.1038/nature19825 Volltext http://search.proquest.com/docview/1838071441 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-SPO SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_11 GBV_ILN_22 GBV_ILN_30 GBV_ILN_40 GBV_ILN_47 GBV_ILN_55 GBV_ILN_59 GBV_ILN_60 GBV_ILN_62 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_101 GBV_ILN_110 GBV_ILN_120 GBV_ILN_154 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_211 GBV_ILN_290 GBV_ILN_294 GBV_ILN_601 GBV_ILN_647 GBV_ILN_754 GBV_ILN_2001 GBV_ILN_2002 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2015 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2026 GBV_ILN_2095 GBV_ILN_2116 GBV_ILN_2120 GBV_ILN_2121 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_2279 GBV_ILN_2286 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4317 GBV_ILN_4320 GBV_ILN_4324 GBV_ILN_4700 AR 539 2016 7627 43-47 |
spelling |
10.1038/nature19825 doi PQ20170301 (DE-627)OLC1984925571 (DE-599)GBVOLC1984925571 (PRQ)c1825-7e411c36e881f0b8b2a3717ea97fe975e7836bf8622b35cffa367683ab5a78c80 (KEY)0072945020160000539762700043novophasingwithxraylaserrevealsmosquitolarvicidebi DE-627 ger DE-627 rakwb eng 070 500 DE-101 500 AVZ BIODIV fid Jacques-Philippe Colletier verfasserin aut De novo phasing with X-ray laser reveals mosquito larvicide BinAB structure 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier BinAB is a naturally occurring paracrystalline larvicide distributed worldwide to combat the devastating diseases borne by mosquitoes. These crystals are composed of homologous molecules, BinA and BinB, which play distinct roles in the multi-step intoxication process, transforming from harmless, robust crystals, to soluble protoxin heterodimers, to internalized mature toxin, and finally to toxic oligomeric pores. The small size of the crystals-50 unit cells per edge, on average-has impeded structural characterization by conventional means. Here we report the structure of Lysinibacillus sphaericus BinAB solved de novo by serial-femtosecond crystallography at an X-ray free-electron laser. The structure reveals tyrosine- and carboxylate-mediated contacts acting as pH switches to release soluble protoxin in the alkaline larval midgut. An enormous heterodimeric interface appears to be responsible for anchoring BinA to receptor-bound BinB for co-internalization. Remarkably, this interface is largely composed of propeptides, suggesting that proteolytic maturation would trigger dissociation of the heterodimer and progression to pore formation. Mosquitoes Crystals Toxicity Pesticides X-ray lasers Pesticide residues Health aspects Structure Observations Usage Michael R Sawaya oth Mari Gingery oth Jose A Rodriguez oth Duilio Cascio oth Aaron S Brewster oth Tara Michels-Clark oth Robert H Hice oth Nicolas Coquelle oth Sébastien Boutet oth Garth J Williams oth Marc Messerschmidt oth Daniel P DePonte oth Raymond G Sierra oth Hartawan Laksmono oth Jason E Koglin oth Mark S Hunter oth Hyun-Woo Park oth Monarin Uervirojnangkoorn oth Dennis K Bideshi oth Axel T Brunger oth Brian A Federici oth Nicholas K Sauter oth David S Eisenberg oth Enthalten in Nature London : Macmillan Publishers Limited, part of Springer Nature, 1869 539(2016), 7627, Seite 43-47 (DE-627)129292834 (DE-600)120714-3 (DE-576)014473941 0028-0836 nnns volume:539 year:2016 number:7627 pages:43-47 http://dx.doi.org/10.1038/nature19825 Volltext http://search.proquest.com/docview/1838071441 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-SPO SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_11 GBV_ILN_22 GBV_ILN_30 GBV_ILN_40 GBV_ILN_47 GBV_ILN_55 GBV_ILN_59 GBV_ILN_60 GBV_ILN_62 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_101 GBV_ILN_110 GBV_ILN_120 GBV_ILN_154 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_211 GBV_ILN_290 GBV_ILN_294 GBV_ILN_601 GBV_ILN_647 GBV_ILN_754 GBV_ILN_2001 GBV_ILN_2002 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2015 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2026 GBV_ILN_2095 GBV_ILN_2116 GBV_ILN_2120 GBV_ILN_2121 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_2279 GBV_ILN_2286 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4317 GBV_ILN_4320 GBV_ILN_4324 GBV_ILN_4700 AR 539 2016 7627 43-47 |
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10.1038/nature19825 doi PQ20170301 (DE-627)OLC1984925571 (DE-599)GBVOLC1984925571 (PRQ)c1825-7e411c36e881f0b8b2a3717ea97fe975e7836bf8622b35cffa367683ab5a78c80 (KEY)0072945020160000539762700043novophasingwithxraylaserrevealsmosquitolarvicidebi DE-627 ger DE-627 rakwb eng 070 500 DE-101 500 AVZ BIODIV fid Jacques-Philippe Colletier verfasserin aut De novo phasing with X-ray laser reveals mosquito larvicide BinAB structure 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier BinAB is a naturally occurring paracrystalline larvicide distributed worldwide to combat the devastating diseases borne by mosquitoes. These crystals are composed of homologous molecules, BinA and BinB, which play distinct roles in the multi-step intoxication process, transforming from harmless, robust crystals, to soluble protoxin heterodimers, to internalized mature toxin, and finally to toxic oligomeric pores. The small size of the crystals-50 unit cells per edge, on average-has impeded structural characterization by conventional means. Here we report the structure of Lysinibacillus sphaericus BinAB solved de novo by serial-femtosecond crystallography at an X-ray free-electron laser. The structure reveals tyrosine- and carboxylate-mediated contacts acting as pH switches to release soluble protoxin in the alkaline larval midgut. An enormous heterodimeric interface appears to be responsible for anchoring BinA to receptor-bound BinB for co-internalization. Remarkably, this interface is largely composed of propeptides, suggesting that proteolytic maturation would trigger dissociation of the heterodimer and progression to pore formation. Mosquitoes Crystals Toxicity Pesticides X-ray lasers Pesticide residues Health aspects Structure Observations Usage Michael R Sawaya oth Mari Gingery oth Jose A Rodriguez oth Duilio Cascio oth Aaron S Brewster oth Tara Michels-Clark oth Robert H Hice oth Nicolas Coquelle oth Sébastien Boutet oth Garth J Williams oth Marc Messerschmidt oth Daniel P DePonte oth Raymond G Sierra oth Hartawan Laksmono oth Jason E Koglin oth Mark S Hunter oth Hyun-Woo Park oth Monarin Uervirojnangkoorn oth Dennis K Bideshi oth Axel T Brunger oth Brian A Federici oth Nicholas K Sauter oth David S Eisenberg oth Enthalten in Nature London : Macmillan Publishers Limited, part of Springer Nature, 1869 539(2016), 7627, Seite 43-47 (DE-627)129292834 (DE-600)120714-3 (DE-576)014473941 0028-0836 nnns volume:539 year:2016 number:7627 pages:43-47 http://dx.doi.org/10.1038/nature19825 Volltext http://search.proquest.com/docview/1838071441 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-SPO SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_11 GBV_ILN_22 GBV_ILN_30 GBV_ILN_40 GBV_ILN_47 GBV_ILN_55 GBV_ILN_59 GBV_ILN_60 GBV_ILN_62 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_101 GBV_ILN_110 GBV_ILN_120 GBV_ILN_154 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_211 GBV_ILN_290 GBV_ILN_294 GBV_ILN_601 GBV_ILN_647 GBV_ILN_754 GBV_ILN_2001 GBV_ILN_2002 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2015 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2026 GBV_ILN_2095 GBV_ILN_2116 GBV_ILN_2120 GBV_ILN_2121 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_2279 GBV_ILN_2286 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4317 GBV_ILN_4320 GBV_ILN_4324 GBV_ILN_4700 AR 539 2016 7627 43-47 |
allfieldsGer |
10.1038/nature19825 doi PQ20170301 (DE-627)OLC1984925571 (DE-599)GBVOLC1984925571 (PRQ)c1825-7e411c36e881f0b8b2a3717ea97fe975e7836bf8622b35cffa367683ab5a78c80 (KEY)0072945020160000539762700043novophasingwithxraylaserrevealsmosquitolarvicidebi DE-627 ger DE-627 rakwb eng 070 500 DE-101 500 AVZ BIODIV fid Jacques-Philippe Colletier verfasserin aut De novo phasing with X-ray laser reveals mosquito larvicide BinAB structure 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier BinAB is a naturally occurring paracrystalline larvicide distributed worldwide to combat the devastating diseases borne by mosquitoes. These crystals are composed of homologous molecules, BinA and BinB, which play distinct roles in the multi-step intoxication process, transforming from harmless, robust crystals, to soluble protoxin heterodimers, to internalized mature toxin, and finally to toxic oligomeric pores. The small size of the crystals-50 unit cells per edge, on average-has impeded structural characterization by conventional means. Here we report the structure of Lysinibacillus sphaericus BinAB solved de novo by serial-femtosecond crystallography at an X-ray free-electron laser. The structure reveals tyrosine- and carboxylate-mediated contacts acting as pH switches to release soluble protoxin in the alkaline larval midgut. An enormous heterodimeric interface appears to be responsible for anchoring BinA to receptor-bound BinB for co-internalization. Remarkably, this interface is largely composed of propeptides, suggesting that proteolytic maturation would trigger dissociation of the heterodimer and progression to pore formation. Mosquitoes Crystals Toxicity Pesticides X-ray lasers Pesticide residues Health aspects Structure Observations Usage Michael R Sawaya oth Mari Gingery oth Jose A Rodriguez oth Duilio Cascio oth Aaron S Brewster oth Tara Michels-Clark oth Robert H Hice oth Nicolas Coquelle oth Sébastien Boutet oth Garth J Williams oth Marc Messerschmidt oth Daniel P DePonte oth Raymond G Sierra oth Hartawan Laksmono oth Jason E Koglin oth Mark S Hunter oth Hyun-Woo Park oth Monarin Uervirojnangkoorn oth Dennis K Bideshi oth Axel T Brunger oth Brian A Federici oth Nicholas K Sauter oth David S Eisenberg oth Enthalten in Nature London : Macmillan Publishers Limited, part of Springer Nature, 1869 539(2016), 7627, Seite 43-47 (DE-627)129292834 (DE-600)120714-3 (DE-576)014473941 0028-0836 nnns volume:539 year:2016 number:7627 pages:43-47 http://dx.doi.org/10.1038/nature19825 Volltext http://search.proquest.com/docview/1838071441 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-SPO SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_11 GBV_ILN_22 GBV_ILN_30 GBV_ILN_40 GBV_ILN_47 GBV_ILN_55 GBV_ILN_59 GBV_ILN_60 GBV_ILN_62 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_101 GBV_ILN_110 GBV_ILN_120 GBV_ILN_154 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_211 GBV_ILN_290 GBV_ILN_294 GBV_ILN_601 GBV_ILN_647 GBV_ILN_754 GBV_ILN_2001 GBV_ILN_2002 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2015 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2026 GBV_ILN_2095 GBV_ILN_2116 GBV_ILN_2120 GBV_ILN_2121 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_2279 GBV_ILN_2286 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4317 GBV_ILN_4320 GBV_ILN_4324 GBV_ILN_4700 AR 539 2016 7627 43-47 |
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10.1038/nature19825 doi PQ20170301 (DE-627)OLC1984925571 (DE-599)GBVOLC1984925571 (PRQ)c1825-7e411c36e881f0b8b2a3717ea97fe975e7836bf8622b35cffa367683ab5a78c80 (KEY)0072945020160000539762700043novophasingwithxraylaserrevealsmosquitolarvicidebi DE-627 ger DE-627 rakwb eng 070 500 DE-101 500 AVZ BIODIV fid Jacques-Philippe Colletier verfasserin aut De novo phasing with X-ray laser reveals mosquito larvicide BinAB structure 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier BinAB is a naturally occurring paracrystalline larvicide distributed worldwide to combat the devastating diseases borne by mosquitoes. These crystals are composed of homologous molecules, BinA and BinB, which play distinct roles in the multi-step intoxication process, transforming from harmless, robust crystals, to soluble protoxin heterodimers, to internalized mature toxin, and finally to toxic oligomeric pores. The small size of the crystals-50 unit cells per edge, on average-has impeded structural characterization by conventional means. Here we report the structure of Lysinibacillus sphaericus BinAB solved de novo by serial-femtosecond crystallography at an X-ray free-electron laser. The structure reveals tyrosine- and carboxylate-mediated contacts acting as pH switches to release soluble protoxin in the alkaline larval midgut. An enormous heterodimeric interface appears to be responsible for anchoring BinA to receptor-bound BinB for co-internalization. Remarkably, this interface is largely composed of propeptides, suggesting that proteolytic maturation would trigger dissociation of the heterodimer and progression to pore formation. Mosquitoes Crystals Toxicity Pesticides X-ray lasers Pesticide residues Health aspects Structure Observations Usage Michael R Sawaya oth Mari Gingery oth Jose A Rodriguez oth Duilio Cascio oth Aaron S Brewster oth Tara Michels-Clark oth Robert H Hice oth Nicolas Coquelle oth Sébastien Boutet oth Garth J Williams oth Marc Messerschmidt oth Daniel P DePonte oth Raymond G Sierra oth Hartawan Laksmono oth Jason E Koglin oth Mark S Hunter oth Hyun-Woo Park oth Monarin Uervirojnangkoorn oth Dennis K Bideshi oth Axel T Brunger oth Brian A Federici oth Nicholas K Sauter oth David S Eisenberg oth Enthalten in Nature London : Macmillan Publishers Limited, part of Springer Nature, 1869 539(2016), 7627, Seite 43-47 (DE-627)129292834 (DE-600)120714-3 (DE-576)014473941 0028-0836 nnns volume:539 year:2016 number:7627 pages:43-47 http://dx.doi.org/10.1038/nature19825 Volltext http://search.proquest.com/docview/1838071441 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-SPO SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_11 GBV_ILN_22 GBV_ILN_30 GBV_ILN_40 GBV_ILN_47 GBV_ILN_55 GBV_ILN_59 GBV_ILN_60 GBV_ILN_62 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_101 GBV_ILN_110 GBV_ILN_120 GBV_ILN_154 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_211 GBV_ILN_290 GBV_ILN_294 GBV_ILN_601 GBV_ILN_647 GBV_ILN_754 GBV_ILN_2001 GBV_ILN_2002 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2015 GBV_ILN_2016 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2026 GBV_ILN_2095 GBV_ILN_2116 GBV_ILN_2120 GBV_ILN_2121 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_2279 GBV_ILN_2286 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4317 GBV_ILN_4320 GBV_ILN_4324 GBV_ILN_4700 AR 539 2016 7627 43-47 |
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Enthalten in Nature 539(2016), 7627, Seite 43-47 volume:539 year:2016 number:7627 pages:43-47 |
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Jacques-Philippe Colletier @@aut@@ Michael R Sawaya @@oth@@ Mari Gingery @@oth@@ Jose A Rodriguez @@oth@@ Duilio Cascio @@oth@@ Aaron S Brewster @@oth@@ Tara Michels-Clark @@oth@@ Robert H Hice @@oth@@ Nicolas Coquelle @@oth@@ Sébastien Boutet @@oth@@ Garth J Williams @@oth@@ Marc Messerschmidt @@oth@@ Daniel P DePonte @@oth@@ Raymond G Sierra @@oth@@ Hartawan Laksmono @@oth@@ Jason E Koglin @@oth@@ Mark S Hunter @@oth@@ Hyun-Woo Park @@oth@@ Monarin Uervirojnangkoorn @@oth@@ Dennis K Bideshi @@oth@@ Axel T Brunger @@oth@@ Brian A Federici @@oth@@ Nicholas K Sauter @@oth@@ David S Eisenberg @@oth@@ |
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2016-01-01T00:00:00Z |
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Jacques-Philippe Colletier ddc 070 ddc 500 fid BIODIV misc Mosquitoes misc Crystals misc Toxicity misc Pesticides misc X-ray lasers misc Pesticide residues misc Health aspects misc Structure misc Observations misc Usage De novo phasing with X-ray laser reveals mosquito larvicide BinAB structure |
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070 500 DE-101 500 AVZ BIODIV fid De novo phasing with X-ray laser reveals mosquito larvicide BinAB structure Mosquitoes Crystals Toxicity Pesticides X-ray lasers Pesticide residues Health aspects Structure Observations Usage |
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De novo phasing with X-ray laser reveals mosquito larvicide BinAB structure |
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BinAB is a naturally occurring paracrystalline larvicide distributed worldwide to combat the devastating diseases borne by mosquitoes. These crystals are composed of homologous molecules, BinA and BinB, which play distinct roles in the multi-step intoxication process, transforming from harmless, robust crystals, to soluble protoxin heterodimers, to internalized mature toxin, and finally to toxic oligomeric pores. The small size of the crystals-50 unit cells per edge, on average-has impeded structural characterization by conventional means. Here we report the structure of Lysinibacillus sphaericus BinAB solved de novo by serial-femtosecond crystallography at an X-ray free-electron laser. The structure reveals tyrosine- and carboxylate-mediated contacts acting as pH switches to release soluble protoxin in the alkaline larval midgut. An enormous heterodimeric interface appears to be responsible for anchoring BinA to receptor-bound BinB for co-internalization. Remarkably, this interface is largely composed of propeptides, suggesting that proteolytic maturation would trigger dissociation of the heterodimer and progression to pore formation. |
abstractGer |
BinAB is a naturally occurring paracrystalline larvicide distributed worldwide to combat the devastating diseases borne by mosquitoes. These crystals are composed of homologous molecules, BinA and BinB, which play distinct roles in the multi-step intoxication process, transforming from harmless, robust crystals, to soluble protoxin heterodimers, to internalized mature toxin, and finally to toxic oligomeric pores. The small size of the crystals-50 unit cells per edge, on average-has impeded structural characterization by conventional means. Here we report the structure of Lysinibacillus sphaericus BinAB solved de novo by serial-femtosecond crystallography at an X-ray free-electron laser. The structure reveals tyrosine- and carboxylate-mediated contacts acting as pH switches to release soluble protoxin in the alkaline larval midgut. An enormous heterodimeric interface appears to be responsible for anchoring BinA to receptor-bound BinB for co-internalization. Remarkably, this interface is largely composed of propeptides, suggesting that proteolytic maturation would trigger dissociation of the heterodimer and progression to pore formation. |
abstract_unstemmed |
BinAB is a naturally occurring paracrystalline larvicide distributed worldwide to combat the devastating diseases borne by mosquitoes. These crystals are composed of homologous molecules, BinA and BinB, which play distinct roles in the multi-step intoxication process, transforming from harmless, robust crystals, to soluble protoxin heterodimers, to internalized mature toxin, and finally to toxic oligomeric pores. The small size of the crystals-50 unit cells per edge, on average-has impeded structural characterization by conventional means. Here we report the structure of Lysinibacillus sphaericus BinAB solved de novo by serial-femtosecond crystallography at an X-ray free-electron laser. The structure reveals tyrosine- and carboxylate-mediated contacts acting as pH switches to release soluble protoxin in the alkaline larval midgut. An enormous heterodimeric interface appears to be responsible for anchoring BinA to receptor-bound BinB for co-internalization. Remarkably, this interface is largely composed of propeptides, suggesting that proteolytic maturation would trigger dissociation of the heterodimer and progression to pore formation. |
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De novo phasing with X-ray laser reveals mosquito larvicide BinAB structure |
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|
score |
7.400075 |