Publicação
Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-β-D-xylanase 10B in complex with xylohexaose
| Resumo: | The cellulosome of Clostridium thermocellum is a highly organized multi-enzyme complex of cellulases and hemicellulases involved in the hydrolysis of plant cell-wall polysaccharides. The bifunctional multi-modular xylanase Xyn10B is one of the hemicellulase components of the C. thermocellum cellulosome. The enzyme contains an internal glycoside hydrolase family 10 catalytic domain (GH10) and a C-terminal family 1 carbohydrate esterase domain (CE1). The N-terminal moiety of Xyn10B (residues 32-551), comprising a carbohydrate-binding module (CBM22-1) and the GH10 E337A mutant, was crystallized in complex with xylohexaose. The crystals belong to the trigonal space group P3221 and contain a dimer in the asymmetric unit. The crystals diffracted to beyond 2.0 Å resolution. |
|---|---|
| Autores principais: | Najmudin, Shabir |
| Outros Autores: | Pinheiro, Benedita A.; Romão, Maria J.; Prates, José A. M.; Fontes, Carlos M. G. A. |
| Assunto: | Clostridium thermocellum Endo-1,4-β-D-xylanase 10B Structural Biology Biophysics Biochemistry Genetics Condensed Matter Physics |
| Ano: | 2008 |
| País: | Portugal |
| Tipo de documento: | artigo |
| Tipo de acesso: | acesso aberto |
| Instituição associada: | Universidade Nova de Lisboa |
| Idioma: | inglês |
| Origem: | Repositório Institucional da UNL |
| _version_ | 1868983137342586880 |
|---|---|
| author | Najmudin, Shabir |
| author2 | Pinheiro, Benedita A. Romão, Maria J. Prates, José A. M. Fontes, Carlos M. G. A. |
| author2_role | author author author author |
| author_facet | Najmudin, Shabir Pinheiro, Benedita A. Romão, Maria J. Prates, José A. M. Fontes, Carlos M. G. A. |
| author_role | author |
| contributor_name_str_mv | DQ - Departamento de Química CQFB-REQUIMTE - Centro de Química Fina e Biotecnologia (Lab. Associado REQUIMTE) Blackwell Publishing Ltd RUN |
| country_str | PT |
| creators_json_txt | [{\"Person.name\":\"Najmudin, Shabir\"},{\"Person.name\":\"Pinheiro, Benedita A.\"},{\"Person.name\":\"Romão, Maria J.\"},{\"Person.name\":\"Prates, José A. M.\"},{\"Person.name\":\"Fontes, Carlos M. G. A.\"}] |
| datacite.contributors.contributor.contributorName.fl_str_mv | DQ - Departamento de Química CQFB-REQUIMTE - Centro de Química Fina e Biotecnologia (Lab. Associado REQUIMTE) Blackwell Publishing Ltd RUN |
| datacite.creators.creator.creatorName.fl_str_mv | Najmudin, Shabir Pinheiro, Benedita A. Romão, Maria J. Prates, José A. M. Fontes, Carlos M. G. A. |
| datacite.date.Accepted.fl_str_mv | 2008-08-18T00:00:00Z |
| datacite.date.available.fl_str_mv | 2019-03-11T23:15:24Z |
| datacite.date.embargoed.fl_str_mv | 2019-03-11T23:15:24Z |
| datacite.rights.fl_str_mv | http://purl.org/coar/access_right/c_abf2 |
| datacite.subjects.subject.fl_str_mv | Clostridium thermocellum Endo-1,4-β-D-xylanase 10B Structural Biology Biophysics Biochemistry Genetics Condensed Matter Physics |
| datacite.titles.title.fl_str_mv | Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-β-D-xylanase 10B in complex with xylohexaose |
| dc.contributor.none.fl_str_mv | DQ - Departamento de Química CQFB-REQUIMTE - Centro de Química Fina e Biotecnologia (Lab. Associado REQUIMTE) Blackwell Publishing Ltd RUN |
| dc.creator.none.fl_str_mv | Najmudin, Shabir Pinheiro, Benedita A. Romão, Maria J. Prates, José A. M. Fontes, Carlos M. G. A. |
| dc.date.Accepted.fl_str_mv | 2008-08-18T00:00:00Z |
| dc.date.available.fl_str_mv | 2019-03-11T23:15:24Z |
| dc.date.embargoed.fl_str_mv | 2019-03-11T23:15:24Z |
| dc.format.none.fl_str_mv | application/pdf |
| dc.identifier.none.fl_str_mv | http://www.scopus.com/inward/record.url?scp=49249121067&partnerID=8YFLogxK |
| dc.language.none.fl_str_mv | eng |
| dc.rights.none.fl_str_mv | http://purl.org/coar/access_right/c_abf2 |
| dc.subject.none.fl_str_mv | Clostridium thermocellum Endo-1,4-β-D-xylanase 10B Structural Biology Biophysics Biochemistry Genetics Condensed Matter Physics |
| dc.title.fl_str_mv | Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-β-D-xylanase 10B in complex with xylohexaose |
| dc.type.none.fl_str_mv | http://purl.org/coar/resource_type/c_6501 |
| description | The cellulosome of Clostridium thermocellum is a highly organized multi-enzyme complex of cellulases and hemicellulases involved in the hydrolysis of plant cell-wall polysaccharides. The bifunctional multi-modular xylanase Xyn10B is one of the hemicellulase components of the C. thermocellum cellulosome. The enzyme contains an internal glycoside hydrolase family 10 catalytic domain (GH10) and a C-terminal family 1 carbohydrate esterase domain (CE1). The N-terminal moiety of Xyn10B (residues 32-551), comprising a carbohydrate-binding module (CBM22-1) and the GH10 E337A mutant, was crystallized in complex with xylohexaose. The crystals belong to the trigonal space group P3221 and contain a dimer in the asymmetric unit. The crystals diffracted to beyond 2.0 Å resolution. |
| dirty | 0 |
| eu_rights_str_mv | openAccess |
| format | article |
| fulltext.url.fl_str_mv | https://run.unl.pt/bitstreams/28eece02-ee8e-4b1f-8aa6-1f1c20645849/download |
| id | run_7945c2f8fd14ff6161985ca6fda59cd6 |
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| inst_facet_str | urn:organizationAcronym:unl{{{_:::_}}}Universidade Nova de Lisboa |
| instacron_str | unl |
| institution | Universidade Nova de Lisboa |
| instname_str | Universidade Nova de Lisboa |
| language | eng |
| network_acronym_str | run |
| network_name_str | Repositório Institucional da UNL |
| oai_identifier_str | oai:run.unl.pt:10362/62997 |
| organization_str_mv | urn:organizationAcronym:unl |
| person_str_mv | Najmudin, Shabir Pinheiro, Benedita A. Romão, Maria J. Prates, José A. M. Fontes, Carlos M. G. A. |
| publishDate | 2008 |
| repo_facet_str | urn:repositoryAcronym:run{{{_:::_}}}Repositório Institucional da UNL |
| reponame_str | Repositório Institucional da UNL |
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| spelling | engenThe cellulosome of Clostridium thermocellum is a highly organized multi-enzyme complex of cellulases and hemicellulases involved in the hydrolysis of plant cell-wall polysaccharides. The bifunctional multi-modular xylanase Xyn10B is one of the hemicellulase components of the C. thermocellum cellulosome. The enzyme contains an internal glycoside hydrolase family 10 catalytic domain (GH10) and a C-terminal family 1 carbohydrate esterase domain (CE1). The N-terminal moiety of Xyn10B (residues 32-551), comprising a carbohydrate-binding module (CBM22-1) and the GH10 E337A mutant, was crystallized in complex with xylohexaose. The crystals belong to the trigonal space group P3221 and contain a dimer in the asymmetric unit. The crystals diffracted to beyond 2.0 Å resolution.application/pdfenPurification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-β-D-xylanase 10B in complex with xylohexaoseNajmudin, ShabirPinheiro, Benedita A.Romão, Maria J.Prates, José A. M.Fontes, Carlos M. G. A.DQ - Departamento de QuímicaCQFB-REQUIMTE - Centro de Química Fina e Biotecnologia (Lab. Associado REQUIMTE)Blackwell Publishing LtdHostingInstitutionOrganizationalRUNe-mailmailto:run@unl.ptrun@unl.ptISSNIsPartOf1744-3091URNIsPartOfPURE: 12012690URNIsPartOfPURE UUID: ac46d39e-66ac-4841-9370-f2522d2ab9c0URNIsPartOfScopus: 49249121067URNIsPartOfPubMed: 18678939URNIsPartOfPubMedCentral: PMC2494957URNIsPartOfWOS: 000258071000009URNIsPartOfORCID: /0000-0002-3004-0543/work/55386350DOIIsPartOf10.1107/S17443091080196962019-03-11T23:15:24Z2008-08-182008-08-18T00:00:00ZURLhttp://www.scopus.com/inward/record.url?scp=49249121067&partnerID=8YFLogxKhttp://purl.org/coar/access_right/c_abf2open accessClostridium thermocellumEndo-1,4-β-D-xylanase 10BStructural BiologyBiophysicsBiochemistryGeneticsCondensed Matter Physics263707 bytesliteraturehttp://purl.org/coar/resource_type/c_6501journal articlehttp://purl.org/coar/access_right/c_abf2application/pdffulltexthttps://run.unl.pt/bitstreams/28eece02-ee8e-4b1f-8aa6-1f1c20645849/download |
| spellingShingle | Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-β-D-xylanase 10B in complex with xylohexaose Najmudin, Shabir Clostridium thermocellum Endo-1,4-β-D-xylanase 10B Structural Biology Biophysics Biochemistry Genetics Condensed Matter Physics |
| status | SINGLETON |
| subject.fl_str_mv | Clostridium thermocellum Endo-1,4-β-D-xylanase 10B Structural Biology Biophysics Biochemistry Genetics Condensed Matter Physics |
| title | Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-β-D-xylanase 10B in complex with xylohexaose |
| title_full | Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-β-D-xylanase 10B in complex with xylohexaose |
| title_fullStr | Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-β-D-xylanase 10B in complex with xylohexaose |
| title_full_unstemmed | Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-β-D-xylanase 10B in complex with xylohexaose |
| title_short | Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-β-D-xylanase 10B in complex with xylohexaose |
| title_sort | Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-β-D-xylanase 10B in complex with xylohexaose |
| topic | Clostridium thermocellum Endo-1,4-β-D-xylanase 10B Structural Biology Biophysics Biochemistry Genetics Condensed Matter Physics |
| topic_facet | Clostridium thermocellum Endo-1,4-β-D-xylanase 10B Structural Biology Biophysics Biochemistry Genetics Condensed Matter Physics |
| url | http://www.scopus.com/inward/record.url?scp=49249121067&partnerID=8YFLogxK |
| visible | 1 |