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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 8
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pubmed:dateCreated |
2008-8-5
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pubmed:abstractText |
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 P3(2)21 and contain a dimer in the asymmetric unit. The crystals diffracted to beyond 2.0 A resolution.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678939-10819965,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678939-11092928,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678939-11478884,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678939-11567147,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678939-11738044,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678939-12876348,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678939-14623971,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678939-14993688,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678939-15299374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678939-15487947,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678939-15572775,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678939-15681871,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678939-15805601,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678939-15913653,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678939-16314409,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678939-16369096,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678939-17360613,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678939-17642511,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678939-5700707,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678939-7664125,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678939-7717969,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678939-7766136
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1744-3091
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
64
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
715-8
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pubmed:dateRevised |
2010-9-21
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pubmed:meshHeading |
pubmed-meshheading:18678939-Amino Acid Sequence,
pubmed-meshheading:18678939-Base Sequence,
pubmed-meshheading:18678939-Clostridium thermocellum,
pubmed-meshheading:18678939-Crystallization,
pubmed-meshheading:18678939-Crystallography, X-Ray,
pubmed-meshheading:18678939-DNA Primers,
pubmed-meshheading:18678939-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:18678939-Endo-1,4-beta Xylanases,
pubmed-meshheading:18678939-Mutagenesis, Site-Directed,
pubmed-meshheading:18678939-Protein Conformation,
pubmed-meshheading:18678939-Xylans
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pubmed:year |
2008
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pubmed:articleTitle |
Purification, crystallization and crystallographic analysis of Clostridium thermocellum endo-1,4-beta-D-xylanase 10B in complex with xylohexaose.
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pubmed:affiliation |
REQUIMTE, Departamento de Química, FCT-UNL, 2829-516 Caparica, Portugal. shabir@dq.fct.unl.pt
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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