1gwm

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[[Image:1gwm.jpg|left|200px]]<br /><applet load="1gwm" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1gwm.jpg|left|200px]]
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caption="1gwm, resolution 1.15&Aring;" />
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'''CARBOHYDRATE BINDING MODULE FAMILY29 COMPLEXED WITH GLUCOHEXAOSE'''<br />
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{{Structure
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|PDB= 1gwm |SIZE=350|CAPTION= <scene name='initialview01'>1gwm</scene>, resolution 1.15&Aring;
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|SITE= <scene name='pdbsite=AC1:Edo+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CARBOHYDRATE BINDING MODULE FAMILY29 COMPLEXED WITH GLUCOHEXAOSE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1GWM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Piromyces_equi Piromyces equi] with <scene name='pdbligand=CO:'>CO</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Edo+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GWM OCA].
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1GWM 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=1GWM OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12391332 12391332]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12391332 12391332]
[[Category: Piromyces equi]]
[[Category: Piromyces equi]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: mannohexaose]]
[[Category: mannohexaose]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:54:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:28:58 2008''

Revision as of 09:29, 20 March 2008


PDB ID 1gwm

Drag the structure with the mouse to rotate
, resolution 1.15Å
Sites:
Ligands: and
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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