1gwm
From Proteopedia
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|PDB= 1gwm |SIZE=350|CAPTION= <scene name='initialview01'>1gwm</scene>, resolution 1.15Å | |PDB= 1gwm |SIZE=350|CAPTION= <scene name='initialview01'>1gwm</scene>, resolution 1.15Å | ||
|SITE= <scene name='pdbsite=AC1:Edo+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Edo+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene> | + | |LIGAND= <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gwm OCA], [http://www.ebi.ac.uk/pdbsum/1gwm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gwm RCSB]</span> | ||
}} | }} | ||
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[[Category: Davies, G J.]] | [[Category: Davies, G J.]] | ||
[[Category: Nurizzo, D.]] | [[Category: Nurizzo, D.]] | ||
| - | [[Category: CO]] | ||
| - | [[Category: EDO]] | ||
[[Category: carbohydrate binding domain]] | [[Category: carbohydrate binding domain]] | ||
[[Category: cellohexaose]] | [[Category: cellohexaose]] | ||
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[[Category: mannohexaose]] | [[Category: mannohexaose]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:52:52 2008'' |
Revision as of 17:52, 30 March 2008
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| , resolution 1.15Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CARBOHYDRATE BINDING MODULE FAMILY29 COMPLEXED WITH GLUCOHEXAOSE
Overview
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.
About this Structure
1GWM is a Single protein structure of sequence from Piromyces equi. Full crystallographic information is available from OCA.
Reference
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
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