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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
22
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pubmed:dateCreated |
2002-10-30
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pubmed:databankReference |
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pubmed:abstractText |
Carbohydrate-protein recognition is central to many biological processes. Enzymes that act on polysaccharide substrates frequently contain noncatalytic domains, "carbohydrate-binding modules" (CBMs), that target the enzyme to the appropriate substrate. CBMs that recognize specific plant structural polysaccharides are often able to accommodate both the variable backbone and the side-chain decorations of heterogeneous ligands. "CBM29" modules, derived from a noncatalytic component of the Piromyces equi cellulase/hemicellulase complex, provide an example of this selective yet flexible recognition. They discriminate strongly against some polysaccharides while remaining relatively promiscuous toward both beta-1,4-linked manno- and cello-oligosaccharides. This feature may reflect preferential, but flexible, targeting toward glucomannans in the plant cell wall. The three-dimensional structure of CBM29-2 and its complexes with cello- and mannohexaose reveal a beta-jelly-roll topology, with an extended binding groove on the concave surface. The orientation of the aromatic residues complements the conformation of the target sugar polymer while accommodation of both manno- and gluco-configured oligo- and polysaccharides is conferred by virtue of the plasticity of the direct interactions from their axial and equatorial 2-hydroxyls, respectively. Such flexible ligand recognition targets the anaerobic fungal complex to a range of different components in the plant cell wall and thus plays a pivotal role in the highly efficient degradation of this composite structure by the microbial eukaryote.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12391332-10089316,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12391332-10455036,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12391332-10704194,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12391332-10819965,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12391332-11341835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12391332-11560933,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12391332-11598143,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12391332-11673472,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12391332-11733998,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12391332-12079353,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12391332-1406248,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12391332-15299374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12391332-15299554,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12391332-15299555,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12391332-15299926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12391332-2757186,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12391332-7493964,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12391332-8377180,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12391332-8687420,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12391332-8918451
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/(1-6)-alpha-glucomannan,
http://linkedlifedata.com/resource/pubmed/chemical/Carbohydrates,
http://linkedlifedata.com/resource/pubmed/chemical/Cellulase,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Mannans,
http://linkedlifedata.com/resource/pubmed/chemical/NCP1 protein, Piromyces equi,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/cellohexaose,
http://linkedlifedata.com/resource/pubmed/chemical/galactomannan,
http://linkedlifedata.com/resource/pubmed/chemical/hemicellulase,
http://linkedlifedata.com/resource/pubmed/chemical/mannopentaose
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
99
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14077-82
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:12391332-Binding Sites,
pubmed-meshheading:12391332-Carbohydrate Sequence,
pubmed-meshheading:12391332-Carbohydrates,
pubmed-meshheading:12391332-Cellulase,
pubmed-meshheading:12391332-Crystallography, X-Ray,
pubmed-meshheading:12391332-Fungal Proteins,
pubmed-meshheading:12391332-Glycoside Hydrolases,
pubmed-meshheading:12391332-Ligands,
pubmed-meshheading:12391332-Mannans,
pubmed-meshheading:12391332-Models, Molecular,
pubmed-meshheading:12391332-Molecular Sequence Data,
pubmed-meshheading:12391332-Oligosaccharides,
pubmed-meshheading:12391332-Piromyces,
pubmed-meshheading:12391332-Protein Structure, Tertiary,
pubmed-meshheading:12391332-Recombinant Fusion Proteins,
pubmed-meshheading:12391332-Substrate Specificity
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pubmed:year |
2002
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pubmed:articleTitle |
Promiscuity in ligand-binding: The three-dimensional structure of a Piromyces carbohydrate-binding module, CBM29-2, in complex with cello- and mannohexaose.
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pubmed:affiliation |
Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5YW, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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