Xyloglucan is recognized by carbohydrate-binding modules that interact with β-glucan chains
| Autor(a) principal: | |
|---|---|
| Data de Publicação: | 2006 |
| Outros Autores: | , , , , , , , , , |
| Tipo de documento: | Artigo |
| Idioma: | eng |
| Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
| Texto Completo: | https://doi.org/10.1074/jbc.M510559200 |
Resumo: | Biotechnology and Biological Sciences Research Council (BB/C005074/1) |
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oai:run.unl.pt:10362/62999 |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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7160 |
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Xyloglucan is recognized by carbohydrate-binding modules that interact with β-glucan chainsBiochemistryMolecular BiologyCell BiologyBiotechnology and Biological Sciences Research Council (BB/C005074/1)Enzyme systems that attack the plant cell wall contain noncatalytic carbohydrate-binding modules (CBMs) that mediate attachment to this composite structure and play a pivotal role in maximizing the hydrolytic process. Although xyloglucan, which includes a backbone of β-1,4-glucan decorated primarily with xylose residues, is a key component of the plant cell wall, CBMs that bind to this polymer have not been identified. Here we showed that the C-terminal domain of the modular Clostridium thermocellum enzyme CtCel9D-Cel44A (formerly known as CelJ) comprises a novel CBM (designated CBM44) that binds with equal affinity to cellulose and xyloglucan. We also showed that accommodation of xyloglucan side chains is a general feature of CBMs that bind to single cellulose chains. The crystal structures of CBM44 and the other CBM (CBM30) in CtCel9D-Cel44A display a β-sandwich fold. The concave face of both CBMs contains a hydrophobic platform comprising three tryptophan residues that can accommodate up to five glucose residues. The orientation of these aromatic residues is such that the bound ligand would adopt the twisted conformation displayed by cello-oligosaccharides in solution. Mutagenesis studies confirmed that the hydrophobic platform located on the concave face of both CBMs mediates ligand recognition. In contrast to other CBMs that bind to single polysaccharide chains, the polar residues in the binding cleft of CBM44 play only a minor role in ligand recognition. The mechanism by which these proteins are able to recognize linear and decorated β-1,4-glucans is discussed based on the structures of CBM44 and the other CBMs that bind single cellulose chains.DQ - Departamento de QuímicaCQFB-REQUIMTE - Centro de Química Fina e Biotecnologia (Lab. Associado REQUIMTE)RUNNajmudin, ShabirGuerreiro, Catarina I. P. D.Carvalho, Ana L.Prates, José A. M.Correia, Márcia A. S.Alves, Victor D.Ferreira, Luís M. A.Romão, Maria J.Gilbert, Harry J.Bolam, David N.Fontes, Carlos M. G. A.2019-03-11T23:15:29Z2006-03-312006-03-31T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article14application/pdfhttps://doi.org/10.1074/jbc.M510559200eng0021-9258PURE: 12015002http://www.scopus.com/inward/record.url?scp=33646840847&partnerID=8YFLogxKhttps://doi.org/10.1074/jbc.M510559200info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-03-11T04:29:46Zoai:run.unl.pt:10362/62999Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:33:50.219920Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
| dc.title.none.fl_str_mv |
Xyloglucan is recognized by carbohydrate-binding modules that interact with β-glucan chains |
| title |
Xyloglucan is recognized by carbohydrate-binding modules that interact with β-glucan chains |
| spellingShingle |
Xyloglucan is recognized by carbohydrate-binding modules that interact with β-glucan chains Najmudin, Shabir Biochemistry Molecular Biology Cell Biology |
| title_short |
Xyloglucan is recognized by carbohydrate-binding modules that interact with β-glucan chains |
| title_full |
Xyloglucan is recognized by carbohydrate-binding modules that interact with β-glucan chains |
| title_fullStr |
Xyloglucan is recognized by carbohydrate-binding modules that interact with β-glucan chains |
| title_full_unstemmed |
Xyloglucan is recognized by carbohydrate-binding modules that interact with β-glucan chains |
| title_sort |
Xyloglucan is recognized by carbohydrate-binding modules that interact with β-glucan chains |
| author |
Najmudin, Shabir |
| author_facet |
Najmudin, Shabir Guerreiro, Catarina I. P. D. Carvalho, Ana L. Prates, José A. M. Correia, Márcia A. S. Alves, Victor D. Ferreira, Luís M. A. Romão, Maria J. Gilbert, Harry J. Bolam, David N. Fontes, Carlos M. G. A. |
| author_role |
author |
| author2 |
Guerreiro, Catarina I. P. D. Carvalho, Ana L. Prates, José A. M. Correia, Márcia A. S. Alves, Victor D. Ferreira, Luís M. A. Romão, Maria J. Gilbert, Harry J. Bolam, David N. Fontes, Carlos M. G. A. |
| author2_role |
author author author author author author author author author author |
| dc.contributor.none.fl_str_mv |
DQ - Departamento de Química CQFB-REQUIMTE - Centro de Química Fina e Biotecnologia (Lab. Associado REQUIMTE) RUN |
| dc.contributor.author.fl_str_mv |
Najmudin, Shabir Guerreiro, Catarina I. P. D. Carvalho, Ana L. Prates, José A. M. Correia, Márcia A. S. Alves, Victor D. Ferreira, Luís M. A. Romão, Maria J. Gilbert, Harry J. Bolam, David N. Fontes, Carlos M. G. A. |
| dc.subject.por.fl_str_mv |
Biochemistry Molecular Biology Cell Biology |
| topic |
Biochemistry Molecular Biology Cell Biology |
| description |
Biotechnology and Biological Sciences Research Council (BB/C005074/1) |
| publishDate |
2006 |
| dc.date.none.fl_str_mv |
2006-03-31 2006-03-31T00:00:00Z 2019-03-11T23:15:29Z |
| 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 |
https://doi.org/10.1074/jbc.M510559200 |
| url |
https://doi.org/10.1074/jbc.M510559200 |
| dc.language.iso.fl_str_mv |
eng |
| language |
eng |
| dc.relation.none.fl_str_mv |
0021-9258 PURE: 12015002 http://www.scopus.com/inward/record.url?scp=33646840847&partnerID=8YFLogxK https://doi.org/10.1074/jbc.M510559200 |
| dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
| eu_rights_str_mv |
openAccess |
| dc.format.none.fl_str_mv |
14 application/pdf |
| dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
| instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
| instacron_str |
RCAAP |
| institution |
RCAAP |
| reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
| collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
| repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799137960088567808 |