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1w8u

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[[Image:1w8u.gif|left|200px]]
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{{Seed}}
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[[Image:1w8u.png|left|200px]]
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{{STRUCTURE_1w8u| PDB=1w8u | SCENE= }}
{{STRUCTURE_1w8u| PDB=1w8u | SCENE= }}
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'''CBM29-2 MUTANT D83A COMPLEXED WITH MANNOHEXAOSE: PROBING THE MECHANISM OF LIGAND RECOGNITION BY FAMILY 29 CARBOHYDRATE BINDING MODULES'''
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===CBM29-2 MUTANT D83A COMPLEXED WITH MANNOHEXAOSE: PROBING THE MECHANISM OF LIGAND RECOGNITION BY FAMILY 29 CARBOHYDRATE BINDING MODULES===
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==Overview==
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The recycling of photosynthetically fixed carbon, by the action of microbial plant cell wall hydrolases, is integral to one of the major geochemical cycles and is of considerable industrial importance. Non-catalytic carbohydrate-binding modules (CBMs) play a key role in this degradative process by targeting hydrolytic enzymes to their cognate substrate within the complex milieu of polysaccharides that comprise the plant cell wall. Family 29 CBMs have, thus far, only been found in an extracellular multienzyme plant cell wall-degrading complex from the anaerobic fungus Piromyces equi, where they exist as a CBM29-1:CBM29-2 tandem. Here we present both the structure of the CBM29-1 partner, at 1.5 A resolution, and examine the importance of hydrophobic stacking interactions as well as direct and solvent-mediated hydrogen bonds in the binding of CBM29-2 to different polysaccharides. CBM29 domains display unusual binding properties, exhibiting specificity for both beta-manno- and beta-gluco-configured ligands such as mannan, cellulose, and glucomannan. Mutagenesis reveals that "stacking" of tryptophan residues in the n and n+2 subsites plays a critical role in ligand binding, whereas the loss of tyrosine-mediated stacking in the n+4 subsite reduces, but does not abrogate, polysaccharide recognition. Direct hydrogen bonds to ligand, such as those provided by Arg-112 and Glu-78, play a pivotal role in the interaction with both mannan and cellulose, whereas removal of water-mediated interactions has comparatively little effect on carbohydrate binding. The interactions of CBM29-2 with the O2 of glucose or mannose contribute little to binding affinity, explaining why this CBM displays dual gluco/manno specificity.
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{{ABSTRACT_PUBMED_15784618}}
==About this Structure==
==About this Structure==
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[[Category: Glucomannan]]
[[Category: Glucomannan]]
[[Category: Mannohexaose]]
[[Category: Mannohexaose]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:19:48 2008''

Revision as of 11:19, 27 July 2008

Image:1w8u.png

Template:STRUCTURE 1w8u

CBM29-2 MUTANT D83A COMPLEXED WITH MANNOHEXAOSE: PROBING THE MECHANISM OF LIGAND RECOGNITION BY FAMILY 29 CARBOHYDRATE BINDING MODULES

Template:ABSTRACT PUBMED 15784618

About this Structure

1W8U is a Single protein structure of sequence from Piromyces equi. Full crystallographic information is available from OCA.

Reference

Probing the mechanism of ligand recognition in family 29 carbohydrate-binding modules., Flint J, Bolam DN, Nurizzo D, Taylor EJ, Williamson MP, Walters C, Davies GJ, Gilbert HJ, J Biol Chem. 2005 Jun 24;280(25):23718-26. Epub 2005 Mar 22. PMID:15784618

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