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1gwl

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<StructureSection load='1gwl' size='340' side='right'caption='[[1gwl]], [[Resolution|resolution]] 1.51&Aring;' scene=''>
<StructureSection load='1gwl' size='340' side='right'caption='[[1gwl]], [[Resolution|resolution]] 1.51&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1gwl]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GWL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GWL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1gwl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Piromyces_sp._'equi' Piromyces sp. 'equi']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GWL FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.51&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gwk|1gwk]], [[1gwm|1gwm]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gwl OCA], [http://pdbe.org/1gwl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gwl RCSB], [http://www.ebi.ac.uk/pdbsum/1gwl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gwl ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gwl OCA], [https://pdbe.org/1gwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gwl RCSB], [https://www.ebi.ac.uk/pdbsum/1gwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gwl ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q9C171_PIREQ Q9C171_PIREQ]
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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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Promiscuity in ligand-binding: The three-dimensional structure of a Piromyces carbohydrate-binding module, CBM29-2, in complex with cello- and mannohexaose.,Charnock SJ, Bolam DN, Nurizzo D, Szabo L, McKie VA, Gilbert HJ, Davies GJ Proc Natl Acad Sci U S A. 2002 Oct 29;99(22):14077-82. Epub 2002 Oct 21. PMID:12391332<ref>PMID:12391332</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1gwl" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Charnock, S J]]
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[[Category: Piromyces sp. 'equi']]
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[[Category: Davies, G J]]
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[[Category: Charnock SJ]]
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[[Category: Nurizzo, D]]
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[[Category: Davies GJ]]
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[[Category: Carbohydrate binding domain]]
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[[Category: Nurizzo D]]
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[[Category: Cellohexaose]]
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[[Category: Cellulosome]]
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[[Category: Glucomannan]]
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[[Category: Mannohexaose]]
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Current revision

Carbohydrate binding module family29 complexed with mannohexaose

PDB ID 1gwl

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