1wcu
From Proteopedia
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| - | [[Image:1wcu.gif|left|200px]] | + | [[Image:1wcu.gif|left|200px]] |
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| - | '''CBM29_1, A FAMILY 29 CARBOHYDRATE BINDING MODULE FROM PIROMYCES EQUI''' | + | {{Structure |
| + | |PDB= 1wcu |SIZE=350|CAPTION= <scene name='initialview01'>1wcu</scene>, resolution 1.50Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CBM29_1, A FAMILY 29 CARBOHYDRATE BINDING MODULE FROM PIROMYCES EQUI''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1WCU is a [ | + | 1WCU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Piromyces_equi Piromyces equi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WCU OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15784618 15784618] |
[[Category: Piromyces equi]] | [[Category: Piromyces equi]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: cbm29_1]] | [[Category: cbm29_1]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:55:19 2008'' |
Revision as of 12:55, 20 March 2008
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| , resolution 1.50Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CBM29_1, A FAMILY 29 CARBOHYDRATE BINDING MODULE FROM PIROMYCES EQUI
Overview
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.
About this Structure
1WCU 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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