3a3h

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[[Image:3a3h.gif|left|200px]]
[[Image:3a3h.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 3a3h |SIZE=350|CAPTION= <scene name='initialview01'>3a3h</scene>, resolution 1.64&Aring;
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The line below this paragraph, containing "STRUCTURE_3a3h", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=ACI:Catalytic+Acid/Base'>ACI</scene> and <scene name='pdbsite=NUC:Catalytic+Nucleophile'>NUC</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CTR:CELLOTRIOSE'>CTR</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_3a3h| PDB=3a3h | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3a3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a3h OCA], [http://www.ebi.ac.uk/pdbsum/3a3h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3a3h RCSB]</span>
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}}
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'''CELLOTRIOSE COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHERANS AT 1.6 A RESOLUTION'''
'''CELLOTRIOSE COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHERANS AT 1.6 A RESOLUTION'''
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[[Category: Davies, G J.]]
[[Category: Davies, G J.]]
[[Category: Schulein, M.]]
[[Category: Schulein, M.]]
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[[Category: cellulose degradation]]
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[[Category: Cellulose degradation]]
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[[Category: endoglucanase]]
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[[Category: Endoglucanase]]
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[[Category: glycoside hydrolase family 5]]
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[[Category: Glycoside hydrolase family 5]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:18:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:22:14 2008''
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Revision as of 17:18, 4 May 2008

Image:3a3h.gif

Template:STRUCTURE 3a3h

CELLOTRIOSE COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHERANS AT 1.6 A RESOLUTION


Overview

The enzymatic hydrolysis of O-glycosidic linkages is one of the most diverse and widespread reactions in nature and involves a classic "textbook" enzyme mechanism. A multidisciplinary analysis of a beta-glycoside hydrolase, the Cel5A from Bacillus agaradhaerens, is presented in which the structures of each of the native, substrate, covalent-intermediate, and product complexes have been determined and their interconversions analyzed kinetically, providing unprecedented insights into the mechanism of this enzyme class. Substrate is bound in a distorted 1S3 skew-boat conformation, thereby presenting the anomeric carbon appropriately for nucleophilic attack as well as satisfying the stereoelectronic requirements for an incipient oxocarbenium ion. Leaving group departure results in the trapping of a covalent alpha-glycosyl-enzyme intermediate in which the sugar adopts an undistorted 4C1 conformation. Finally, hydrolysis of this intermediate yields a product complex in which the sugar is bound in a partially disordered mode, consistent with unfavorable interactions and low product affinity.

About this Structure

3A3H is a Single protein structure of sequence from Bacillus agaradhaerens. Full crystallographic information is available from OCA.

Reference

Snapshots along an enzymatic reaction coordinate: analysis of a retaining beta-glycoside hydrolase., Davies GJ, Mackenzie L, Varrot A, Dauter M, Brzozowski AM, Schulein M, Withers SG, Biochemistry. 1998 Aug 25;37(34):11707-13. PMID:9718293 Page seeded by OCA on Sun May 4 20:18:55 2008

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