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2exo

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[[Image:2exo.jpg|left|200px]]<br /><applet load="2exo" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2exo.jpg|left|200px]]
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caption="2exo, resolution 1.8&Aring;" />
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'''CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF THE BETA-1,4-GLYCANASE CEX FROM CELLULOMONAS FIMI'''<br />
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{{Structure
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|PDB= 2exo |SIZE=350|CAPTION= <scene name='initialview01'>2exo</scene>, resolution 1.8&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase Cellulose 1,4-beta-cellobiosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF THE BETA-1,4-GLYCANASE CEX FROM CELLULOMONAS FIMI'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2EXO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]. Active as [http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase Cellulose 1,4-beta-cellobiosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EXO OCA].
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2EXO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EXO OCA].
==Reference==
==Reference==
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Crystal structure of the catalytic domain of the beta-1,4-glycanase cex from Cellulomonas fimi., White A, Withers SG, Gilkes NR, Rose DR, Biochemistry. 1994 Oct 25;33(42):12546-52. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7918478 7918478]
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Crystal structure of the catalytic domain of the beta-1,4-glycanase cex from Cellulomonas fimi., White A, Withers SG, Gilkes NR, Rose DR, Biochemistry. 1994 Oct 25;33(42):12546-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7918478 7918478]
[[Category: Cellulomonas fimi]]
[[Category: Cellulomonas fimi]]
[[Category: Cellulose 1,4-beta-cellobiosidase]]
[[Category: Cellulose 1,4-beta-cellobiosidase]]
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[[Category: hydrolase (o-glycosyl)]]
[[Category: hydrolase (o-glycosyl)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:15:37 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:45:41 2008''

Revision as of 14:45, 20 March 2008


PDB ID 2exo

Drag the structure with the mouse to rotate
, resolution 1.8Å
Activity: Cellulose 1,4-beta-cellobiosidase, with EC number 3.2.1.91
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF THE BETA-1,4-GLYCANASE CEX FROM CELLULOMONAS FIMI


Overview

beta-1,4-Glycanases, principally cellulases and xylanases, are responsible for the hydrolysis of plant biomass. The bifunctional beta-1,4-xylanase/glucanase Cex from the bacterium Cellulomonas fimi, one of a large family of cellulases/xylanases, depolymerizes oligosaccharides and releases a disaccharide unit from the substrate nonreducing end. Hydrolysis occurs with net retention of the anomeric configuration of the sugar through a double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. The active site nucleophile, Glu233, has been unambiguously identified by trapping of such an intermediate [Tull et al. (1991) J. Biol. Chem. 266, 15621-15625] and the acid/base catalyst, Glu127, by detailed kinetic analysis of mutants [MacLeod et al. (1994) Biochemistry 33, 6371-6376]. However, little is known about the enzyme's overall folding and its active site architecture. We report here the high-resolution crystal structure of the catalytic domain of Cex. The atomic structure refinement results in a model that includes 2400 protein atoms and 45 water molecules, with an R-factor of 0.217 for data extending to 1.8-A resolution. The protein forms an eight-parallel-stranded alpha/beta-barrel, which is a novel folding pattern for a microbial beta-glycanase. The active site, inferred from the location of Glu233, Glu127, and other conserved residues, is an open cleft on the carboxy-terminal end of the alpha/beta-barrel. An extensive hydrogen-bonding network stabilizes the ionization states of the key residues; in particular, the Asp235-His205-Glu233 hydrogen-bonding network may play a role in modulating the ionization state of Glu233 and in controlling local charge balance during the reaction.

About this Structure

2EXO is a Single protein structure of sequence from Cellulomonas fimi. Full crystallographic information is available from OCA.

Reference

Crystal structure of the catalytic domain of the beta-1,4-glycanase cex from Cellulomonas fimi., White A, Withers SG, Gilkes NR, Rose DR, Biochemistry. 1994 Oct 25;33(42):12546-52. PMID:7918478

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