Structural Analysis of the Partially Disordered Protein EspK from <i<Mycobacterium Tuberculosis</i<

For centuries, tuberculosis has been a worldwide burden for human health, and gaps in our understanding of its pathogenesis have hampered the development of new treatments. ESX-1 is a complex machinery responsible for the secretion of virulence factors that manipulate the host response. Despite the...
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Autor*in:	Abril Gijsbers [verfasserIn] Nuria Sánchez-Puig [verfasserIn] Ye Gao [verfasserIn] Peter J. Peters [verfasserIn] Raimond B. G. Ravelli [verfasserIn] Dritan Siliqi [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2020

Schlagwörter:	disordered region EspK ESX-1 SAXS

Übergeordnetes Werk:	In: Crystals - MDPI AG, 2011, 11(2020), 1, p 18
Übergeordnetes Werk:	volume:11 ; year:2020 ; number:1, p 18

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/cryst11010018

Katalog-ID:	DOAJ087108712

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allfieldsGer	10.3390/cryst11010018 doi (DE-627)DOAJ087108712 (DE-599)DOAJ8d83196956f14cc28472aff1fc639e3b DE-627 ger DE-627 rakwb eng QD901-999 Abril Gijsbers verfasserin aut Structural Analysis of the Partially Disordered Protein EspK from <i<Mycobacterium Tuberculosis</i< 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier For centuries, tuberculosis has been a worldwide burden for human health, and gaps in our understanding of its pathogenesis have hampered the development of new treatments. ESX-1 is a complex machinery responsible for the secretion of virulence factors that manipulate the host response. Despite the importance of these secreted proteins for pathogenicity, only a few of them have been structurally and functionally characterised. Here, we describe a structural study of the ESX-secretion associated protein K (EspK), a 74 kDa protein known to be essential for the secretion of other substrates and the cytolytic effects of ESX-1. Small-Angle X-ray Scattering (SAXS) data show that EspK is a long molecule with a maximal dimension of 228 Å. It consists of two independent folded regions at each end of the protein connected by a flexible unstructured region driving the protein to coexist as an ensemble of conformations. Limited proteolysis identified a 26 kDa globular domain at the C-terminus of the protein consisting of a mixture of α-helices and β-strands, as shown by circular dichroism (CD) and SAXS. In contrast, the N-terminal portion is mainly helical with an elongated shape. Sequence conservation suggests that this architecture is preserved amongst the different mycobacteria species, proposing specific roles for the N- and C-terminal domains assisted by the middle flexible linker. disordered region EspK ESX-1 SAXS Crystallography Nuria Sánchez-Puig verfasserin aut Ye Gao verfasserin aut Peter J. Peters verfasserin aut Raimond B. G. Ravelli verfasserin aut Dritan Siliqi verfasserin aut In Crystals MDPI AG, 2011 11(2020), 1, p 18 (DE-627)718303067 (DE-600)2661516-2 20734352 nnns volume:11 year:2020 number:1, p 18 https://doi.org/10.3390/cryst11010018 kostenfrei https://doaj.org/article/8d83196956f14cc28472aff1fc639e3b kostenfrei https://www.mdpi.com/2073-4352/11/1/18 kostenfrei https://doaj.org/toc/2073-4352 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_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2055 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_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2020 1, p 18
allfieldsSound	10.3390/cryst11010018 doi (DE-627)DOAJ087108712 (DE-599)DOAJ8d83196956f14cc28472aff1fc639e3b DE-627 ger DE-627 rakwb eng QD901-999 Abril Gijsbers verfasserin aut Structural Analysis of the Partially Disordered Protein EspK from <i<Mycobacterium Tuberculosis</i< 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier For centuries, tuberculosis has been a worldwide burden for human health, and gaps in our understanding of its pathogenesis have hampered the development of new treatments. ESX-1 is a complex machinery responsible for the secretion of virulence factors that manipulate the host response. Despite the importance of these secreted proteins for pathogenicity, only a few of them have been structurally and functionally characterised. Here, we describe a structural study of the ESX-secretion associated protein K (EspK), a 74 kDa protein known to be essential for the secretion of other substrates and the cytolytic effects of ESX-1. Small-Angle X-ray Scattering (SAXS) data show that EspK is a long molecule with a maximal dimension of 228 Å. It consists of two independent folded regions at each end of the protein connected by a flexible unstructured region driving the protein to coexist as an ensemble of conformations. Limited proteolysis identified a 26 kDa globular domain at the C-terminus of the protein consisting of a mixture of α-helices and β-strands, as shown by circular dichroism (CD) and SAXS. In contrast, the N-terminal portion is mainly helical with an elongated shape. Sequence conservation suggests that this architecture is preserved amongst the different mycobacteria species, proposing specific roles for the N- and C-terminal domains assisted by the middle flexible linker. disordered region EspK ESX-1 SAXS Crystallography Nuria Sánchez-Puig verfasserin aut Ye Gao verfasserin aut Peter J. Peters verfasserin aut Raimond B. G. Ravelli verfasserin aut Dritan Siliqi verfasserin aut In Crystals MDPI AG, 2011 11(2020), 1, p 18 (DE-627)718303067 (DE-600)2661516-2 20734352 nnns volume:11 year:2020 number:1, p 18 https://doi.org/10.3390/cryst11010018 kostenfrei https://doaj.org/article/8d83196956f14cc28472aff1fc639e3b kostenfrei https://www.mdpi.com/2073-4352/11/1/18 kostenfrei https://doaj.org/toc/2073-4352 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_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2055 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_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2020 1, p 18
language	English
source	In Crystals 11(2020), 1, p 18 volume:11 year:2020 number:1, p 18
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topic_facet	disordered region EspK ESX-1 SAXS Crystallography
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container_title	Crystals
authorswithroles_txt_mv	Abril Gijsbers @@aut@@ Nuria Sánchez-Puig @@aut@@ Ye Gao @@aut@@ Peter J. Peters @@aut@@ Raimond B. G. Ravelli @@aut@@ Dritan Siliqi @@aut@@
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callnumber-first	Q - Science
author	Abril Gijsbers
spellingShingle	Abril Gijsbers misc QD901-999 misc disordered region misc EspK misc ESX-1 misc SAXS misc Crystallography Structural Analysis of the Partially Disordered Protein EspK from <i<Mycobacterium Tuberculosis</i<
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topic_title	QD901-999 Structural Analysis of the Partially Disordered Protein EspK from <i<Mycobacterium Tuberculosis</i< disordered region EspK ESX-1 SAXS
topic	misc QD901-999 misc disordered region misc EspK misc ESX-1 misc SAXS misc Crystallography
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title	Structural Analysis of the Partially Disordered Protein EspK from <i<Mycobacterium Tuberculosis</i<
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author_browse	Abril Gijsbers Nuria Sánchez-Puig Ye Gao Peter J. Peters Raimond B. G. Ravelli Dritan Siliqi
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title_sort	structural analysis of the partially disordered protein espk from <i<mycobacterium tuberculosis</i<
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title_auth	Structural Analysis of the Partially Disordered Protein EspK from <i<Mycobacterium Tuberculosis</i<
abstract	For centuries, tuberculosis has been a worldwide burden for human health, and gaps in our understanding of its pathogenesis have hampered the development of new treatments. ESX-1 is a complex machinery responsible for the secretion of virulence factors that manipulate the host response. Despite the importance of these secreted proteins for pathogenicity, only a few of them have been structurally and functionally characterised. Here, we describe a structural study of the ESX-secretion associated protein K (EspK), a 74 kDa protein known to be essential for the secretion of other substrates and the cytolytic effects of ESX-1. Small-Angle X-ray Scattering (SAXS) data show that EspK is a long molecule with a maximal dimension of 228 Å. It consists of two independent folded regions at each end of the protein connected by a flexible unstructured region driving the protein to coexist as an ensemble of conformations. Limited proteolysis identified a 26 kDa globular domain at the C-terminus of the protein consisting of a mixture of α-helices and β-strands, as shown by circular dichroism (CD) and SAXS. In contrast, the N-terminal portion is mainly helical with an elongated shape. Sequence conservation suggests that this architecture is preserved amongst the different mycobacteria species, proposing specific roles for the N- and C-terminal domains assisted by the middle flexible linker.
abstractGer	For centuries, tuberculosis has been a worldwide burden for human health, and gaps in our understanding of its pathogenesis have hampered the development of new treatments. ESX-1 is a complex machinery responsible for the secretion of virulence factors that manipulate the host response. Despite the importance of these secreted proteins for pathogenicity, only a few of them have been structurally and functionally characterised. Here, we describe a structural study of the ESX-secretion associated protein K (EspK), a 74 kDa protein known to be essential for the secretion of other substrates and the cytolytic effects of ESX-1. Small-Angle X-ray Scattering (SAXS) data show that EspK is a long molecule with a maximal dimension of 228 Å. It consists of two independent folded regions at each end of the protein connected by a flexible unstructured region driving the protein to coexist as an ensemble of conformations. Limited proteolysis identified a 26 kDa globular domain at the C-terminus of the protein consisting of a mixture of α-helices and β-strands, as shown by circular dichroism (CD) and SAXS. In contrast, the N-terminal portion is mainly helical with an elongated shape. Sequence conservation suggests that this architecture is preserved amongst the different mycobacteria species, proposing specific roles for the N- and C-terminal domains assisted by the middle flexible linker.
abstract_unstemmed	For centuries, tuberculosis has been a worldwide burden for human health, and gaps in our understanding of its pathogenesis have hampered the development of new treatments. ESX-1 is a complex machinery responsible for the secretion of virulence factors that manipulate the host response. Despite the importance of these secreted proteins for pathogenicity, only a few of them have been structurally and functionally characterised. Here, we describe a structural study of the ESX-secretion associated protein K (EspK), a 74 kDa protein known to be essential for the secretion of other substrates and the cytolytic effects of ESX-1. Small-Angle X-ray Scattering (SAXS) data show that EspK is a long molecule with a maximal dimension of 228 Å. It consists of two independent folded regions at each end of the protein connected by a flexible unstructured region driving the protein to coexist as an ensemble of conformations. Limited proteolysis identified a 26 kDa globular domain at the C-terminus of the protein consisting of a mixture of α-helices and β-strands, as shown by circular dichroism (CD) and SAXS. In contrast, the N-terminal portion is mainly helical with an elongated shape. Sequence conservation suggests that this architecture is preserved amongst the different mycobacteria species, proposing specific roles for the N- and C-terminal domains assisted by the middle flexible linker.
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title_short	Structural Analysis of the Partially Disordered Protein EspK from <i<Mycobacterium Tuberculosis</i<
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Structural Analysis of the Partially Disordered Protein EspK from <i<Mycobacterium Tuberculosis</i<

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