Crystallization and preliminary X-ray diffraction analysis of Xyn30D from Paenibacillus barcinonensis

Xyn30D, a new member of a recently identified group of xylanases, has been purified and crystallized. Xyn30D is a bimodular enzyme composed of an N-terminal catalytic domain belonging to glycoside hydrolase family 30 (GH30) and a C-terminal family 35 carbohydrate-binding domain (CBM35) able to bind...

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Autores: Sainz Polo, M. A., Valenzuela Mayorga, Susana Valeria, Pastor Blasco, Francisco I. Javier, Sanz Aparicio, J.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2014
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/59423
Acceso en línea:https://hdl.handle.net/2445/59423
Access Level:acceso abierto
Palabra clave:Enzims microbians
Biopolímers
Microbial enzymes
Biopolymers
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spelling Crystallization and preliminary X-ray diffraction analysis of Xyn30D from Paenibacillus barcinonensisSainz Polo, M. A.Valenzuela Mayorga, Susana ValeriaPastor Blasco, Francisco I. JavierSanz Aparicio, J.Enzims microbiansBiopolímersMicrobial enzymesBiopolymersXyn30D, a new member of a recently identified group of xylanases, has been purified and crystallized. Xyn30D is a bimodular enzyme composed of an N-terminal catalytic domain belonging to glycoside hydrolase family 30 (GH30) and a C-terminal family 35 carbohydrate-binding domain (CBM35) able to bind xylans and glucuronic acid. Xyn30D shares the characteristic endo mode of action described for GH30 xylanases, with the hydrolysis of the [beta]-(1,4) bonds of xylan being directed by [alpha]-1,2-linked glucuronate moieties, which have to be placed at the -2 subsite of the xylanase active site. Crystals of the complete enzyme were obtained and a full data set to 2.3 Å resolution was collected using a synchrotron X-ray source. This represents the first bimodular enzyme with the domain architecture GH30-CBM35. This study will contribute to the understanding of the role that the different xylanases play in the depolymerization of glucuronoxylan.International Union of Crystallography2014info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://hdl.handle.net/2445/59423Articles publicats en revistes (Genètica, Microbiologia i Estadística)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésReproducció del document publicat a: http://dx.doi.org/10.1107/S2053230X14012035Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 2014, vol. F70, p. 963-966http://dx.doi.org/10.1107/S2053230X14012035(c) International Union of Crystallography, 2014info:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/594232026-05-27T06:46:51Z
dc.title.none.fl_str_mv Crystallization and preliminary X-ray diffraction analysis of Xyn30D from Paenibacillus barcinonensis
title Crystallization and preliminary X-ray diffraction analysis of Xyn30D from Paenibacillus barcinonensis
spellingShingle Crystallization and preliminary X-ray diffraction analysis of Xyn30D from Paenibacillus barcinonensis
Sainz Polo, M. A.
Enzims microbians
Biopolímers
Microbial enzymes
Biopolymers
title_short Crystallization and preliminary X-ray diffraction analysis of Xyn30D from Paenibacillus barcinonensis
title_full Crystallization and preliminary X-ray diffraction analysis of Xyn30D from Paenibacillus barcinonensis
title_fullStr Crystallization and preliminary X-ray diffraction analysis of Xyn30D from Paenibacillus barcinonensis
title_full_unstemmed Crystallization and preliminary X-ray diffraction analysis of Xyn30D from Paenibacillus barcinonensis
title_sort Crystallization and preliminary X-ray diffraction analysis of Xyn30D from Paenibacillus barcinonensis
dc.creator.none.fl_str_mv Sainz Polo, M. A.
Valenzuela Mayorga, Susana Valeria
Pastor Blasco, Francisco I. Javier
Sanz Aparicio, J.
author Sainz Polo, M. A.
author_facet Sainz Polo, M. A.
Valenzuela Mayorga, Susana Valeria
Pastor Blasco, Francisco I. Javier
Sanz Aparicio, J.
author_role author
author2 Valenzuela Mayorga, Susana Valeria
Pastor Blasco, Francisco I. Javier
Sanz Aparicio, J.
author2_role author
author
author
dc.subject.none.fl_str_mv Enzims microbians
Biopolímers
Microbial enzymes
Biopolymers
topic Enzims microbians
Biopolímers
Microbial enzymes
Biopolymers
description Xyn30D, a new member of a recently identified group of xylanases, has been purified and crystallized. Xyn30D is a bimodular enzyme composed of an N-terminal catalytic domain belonging to glycoside hydrolase family 30 (GH30) and a C-terminal family 35 carbohydrate-binding domain (CBM35) able to bind xylans and glucuronic acid. Xyn30D shares the characteristic endo mode of action described for GH30 xylanases, with the hydrolysis of the [beta]-(1,4) bonds of xylan being directed by [alpha]-1,2-linked glucuronate moieties, which have to be placed at the -2 subsite of the xylanase active site. Crystals of the complete enzyme were obtained and a full data set to 2.3 Å resolution was collected using a synchrotron X-ray source. This represents the first bimodular enzyme with the domain architecture GH30-CBM35. This study will contribute to the understanding of the role that the different xylanases play in the depolymerization of glucuronoxylan.
publishDate 2014
dc.date.none.fl_str_mv 2014
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/59423
url https://hdl.handle.net/2445/59423
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: http://dx.doi.org/10.1107/S2053230X14012035
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 2014, vol. F70, p. 963-966
http://dx.doi.org/10.1107/S2053230X14012035
dc.rights.none.fl_str_mv (c) International Union of Crystallography, 2014
info:eu-repo/semantics/openAccess
rights_invalid_str_mv (c) International Union of Crystallography, 2014
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv International Union of Crystallography
publisher.none.fl_str_mv International Union of Crystallography
dc.source.none.fl_str_mv Articles publicats en revistes (Genètica, Microbiologia i Estadística)
reponame:Dipòsit Digital de la UB
instname:Universidad de Barcelona
instname_str Universidad de Barcelona
reponame_str Dipòsit Digital de la UB
collection Dipòsit Digital de la UB
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,300724

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