Crystal Structures of Xanthomonas Small Heat Shock Protein Provide a Structural Basis for an Active Molecular Chaperone Oligomer
Autor(a) principal: | |
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Data de Publicação: | 2011 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1016/j.jmb.2011.02.004 http://hdl.handle.net/11449/25360 |
Resumo: | Small heat shock proteins (sHsps) are ubiquitous low-molecular-weight chaperones that prevent protein aggregation under cellular stresses. sHsps contain a structurally conserved alpha-crystallin domain (ACD) of about 100 amino acid residues flanked by varied N- and C-terminal extensions and usually exist as oligomers. Oligomerization is important for the biological functions of most sHsps. However, the active oligomeric states of sHsps are not defined yet. We present here crystal structures (up to 1.65 angstrom resolution) of the sHspA from the plant pathogen Xanthomonas (XaHspA). XaHspA forms closed or open trimers of dimers (hexamers) in crystals but exists predominantly as 36mers in solution as estimated by size-exclusion chromatography. The XaHspA monomer structures mainly consist of alpha-crystallin domain with disordered N- and C-terminal extensions, indicating that the extensions are flexible and not essential for the formation of dimers and 36mers. Under reducing conditions where a-lactalbumin (LA) unfolds and aggregates, XaHspA 36mers formed complexes with one LA per XaHspA dimer. Based on XaHspA dimer dimer interactions observed in crystals, we propose that XaHspA 36mers have four possible conformations, but only XaHspA 36merB, which is formed by open hexamers in 12mer-6mer-6mer-12mer with protruding dimers accessible for substrate (unfolding protein) binding, can bind to 18 reduced LA molecules. Together, our results unravel the structural basis of an active sHsp oligomer. (C) 2011 Elsevier Ltd. All rights reserved. |
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Crystal Structures of Xanthomonas Small Heat Shock Protein Provide a Structural Basis for an Active Molecular Chaperone Oligomeralpha-crystallin domainprotein foldingcataractscitrus cankerheat shock responseSmall heat shock proteins (sHsps) are ubiquitous low-molecular-weight chaperones that prevent protein aggregation under cellular stresses. sHsps contain a structurally conserved alpha-crystallin domain (ACD) of about 100 amino acid residues flanked by varied N- and C-terminal extensions and usually exist as oligomers. Oligomerization is important for the biological functions of most sHsps. However, the active oligomeric states of sHsps are not defined yet. We present here crystal structures (up to 1.65 angstrom resolution) of the sHspA from the plant pathogen Xanthomonas (XaHspA). XaHspA forms closed or open trimers of dimers (hexamers) in crystals but exists predominantly as 36mers in solution as estimated by size-exclusion chromatography. The XaHspA monomer structures mainly consist of alpha-crystallin domain with disordered N- and C-terminal extensions, indicating that the extensions are flexible and not essential for the formation of dimers and 36mers. Under reducing conditions where a-lactalbumin (LA) unfolds and aggregates, XaHspA 36mers formed complexes with one LA per XaHspA dimer. Based on XaHspA dimer dimer interactions observed in crystals, we propose that XaHspA 36mers have four possible conformations, but only XaHspA 36merB, which is formed by open hexamers in 12mer-6mer-6mer-12mer with protruding dimers accessible for substrate (unfolding protein) binding, can bind to 18 reduced LA molecules. Together, our results unravel the structural basis of an active sHsp oligomer. (C) 2011 Elsevier Ltd. All rights reserved.University of California RiversideFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Structural Molecular Biology NetworkLaboratório Nacional de Luz Síncrotron (LNLS)Univ Calif Riverside, Dept Biochem, Riverside, CA 92521 USALNLS, Ctr Biol Mol & Estrutural, BR-13083970 Campinas, SP, BrazilUNESP, Inst Quim, Det Bioquim & Tecnol Quim, BR-14800900 Araraquara, SP, BrazilUNESP, Inst Quim, Det Bioquim & Tecnol Quim, BR-14800900 Araraquara, SP, BrazilFAPESP: 01/07536-6FAPESP: 03/01646-0Academic Press Ltd Elsevier B.V. LtdUniversity of California, Riverside (UCR)LNLSUniversidade Estadual Paulista (Unesp)Hilario, EduardoMedrano Martin, Francisco JavierBertolini, Maria Celia [UNESP]Fan, Li2014-05-20T14:17:54Z2014-05-20T14:17:54Z2011-04-22info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article74-86application/pdfhttp://dx.doi.org/10.1016/j.jmb.2011.02.004Journal of Molecular Biology. London: Academic Press Ltd- Elsevier B.V. Ltd, v. 408, n. 1, p. 74-86, 2011.0022-2836http://hdl.handle.net/11449/2536010.1016/j.jmb.2011.02.004WOS:000289813700007WOS000289813700007.pdf8817669953838863Web of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengJournal of Molecular Biology4.8943,393info:eu-repo/semantics/openAccess2023-12-22T06:24:04Zoai:repositorio.unesp.br:11449/25360Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T21:02:02.065922Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Crystal Structures of Xanthomonas Small Heat Shock Protein Provide a Structural Basis for an Active Molecular Chaperone Oligomer |
title |
Crystal Structures of Xanthomonas Small Heat Shock Protein Provide a Structural Basis for an Active Molecular Chaperone Oligomer |
spellingShingle |
Crystal Structures of Xanthomonas Small Heat Shock Protein Provide a Structural Basis for an Active Molecular Chaperone Oligomer Hilario, Eduardo alpha-crystallin domain protein folding cataracts citrus canker heat shock response |
title_short |
Crystal Structures of Xanthomonas Small Heat Shock Protein Provide a Structural Basis for an Active Molecular Chaperone Oligomer |
title_full |
Crystal Structures of Xanthomonas Small Heat Shock Protein Provide a Structural Basis for an Active Molecular Chaperone Oligomer |
title_fullStr |
Crystal Structures of Xanthomonas Small Heat Shock Protein Provide a Structural Basis for an Active Molecular Chaperone Oligomer |
title_full_unstemmed |
Crystal Structures of Xanthomonas Small Heat Shock Protein Provide a Structural Basis for an Active Molecular Chaperone Oligomer |
title_sort |
Crystal Structures of Xanthomonas Small Heat Shock Protein Provide a Structural Basis for an Active Molecular Chaperone Oligomer |
author |
Hilario, Eduardo |
author_facet |
Hilario, Eduardo Medrano Martin, Francisco Javier Bertolini, Maria Celia [UNESP] Fan, Li |
author_role |
author |
author2 |
Medrano Martin, Francisco Javier Bertolini, Maria Celia [UNESP] Fan, Li |
author2_role |
author author author |
dc.contributor.none.fl_str_mv |
University of California, Riverside (UCR) LNLS Universidade Estadual Paulista (Unesp) |
dc.contributor.author.fl_str_mv |
Hilario, Eduardo Medrano Martin, Francisco Javier Bertolini, Maria Celia [UNESP] Fan, Li |
dc.subject.por.fl_str_mv |
alpha-crystallin domain protein folding cataracts citrus canker heat shock response |
topic |
alpha-crystallin domain protein folding cataracts citrus canker heat shock response |
description |
Small heat shock proteins (sHsps) are ubiquitous low-molecular-weight chaperones that prevent protein aggregation under cellular stresses. sHsps contain a structurally conserved alpha-crystallin domain (ACD) of about 100 amino acid residues flanked by varied N- and C-terminal extensions and usually exist as oligomers. Oligomerization is important for the biological functions of most sHsps. However, the active oligomeric states of sHsps are not defined yet. We present here crystal structures (up to 1.65 angstrom resolution) of the sHspA from the plant pathogen Xanthomonas (XaHspA). XaHspA forms closed or open trimers of dimers (hexamers) in crystals but exists predominantly as 36mers in solution as estimated by size-exclusion chromatography. The XaHspA monomer structures mainly consist of alpha-crystallin domain with disordered N- and C-terminal extensions, indicating that the extensions are flexible and not essential for the formation of dimers and 36mers. Under reducing conditions where a-lactalbumin (LA) unfolds and aggregates, XaHspA 36mers formed complexes with one LA per XaHspA dimer. Based on XaHspA dimer dimer interactions observed in crystals, we propose that XaHspA 36mers have four possible conformations, but only XaHspA 36merB, which is formed by open hexamers in 12mer-6mer-6mer-12mer with protruding dimers accessible for substrate (unfolding protein) binding, can bind to 18 reduced LA molecules. Together, our results unravel the structural basis of an active sHsp oligomer. (C) 2011 Elsevier Ltd. All rights reserved. |
publishDate |
2011 |
dc.date.none.fl_str_mv |
2011-04-22 2014-05-20T14:17:54Z 2014-05-20T14:17:54Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1016/j.jmb.2011.02.004 Journal of Molecular Biology. London: Academic Press Ltd- Elsevier B.V. Ltd, v. 408, n. 1, p. 74-86, 2011. 0022-2836 http://hdl.handle.net/11449/25360 10.1016/j.jmb.2011.02.004 WOS:000289813700007 WOS000289813700007.pdf 8817669953838863 |
url |
http://dx.doi.org/10.1016/j.jmb.2011.02.004 http://hdl.handle.net/11449/25360 |
identifier_str_mv |
Journal of Molecular Biology. London: Academic Press Ltd- Elsevier B.V. Ltd, v. 408, n. 1, p. 74-86, 2011. 0022-2836 10.1016/j.jmb.2011.02.004 WOS:000289813700007 WOS000289813700007.pdf 8817669953838863 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Journal of Molecular Biology 4.894 3,393 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
74-86 application/pdf |
dc.publisher.none.fl_str_mv |
Academic Press Ltd Elsevier B.V. Ltd |
publisher.none.fl_str_mv |
Academic Press Ltd Elsevier B.V. Ltd |
dc.source.none.fl_str_mv |
Web of Science reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808129275698610176 |