5a3h

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[[Image:5a3h.gif|left|200px]]<br /><applet load="5a3h" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:5a3h.gif|left|200px]]
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caption="5a3h, resolution 1.82&Aring;" />
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'''2-DEOXY-2-FLURO-B-D-CELLOBIOSYL/ENZYME INTERMEDIATE COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHEARANS AT 1.8 ANGSTROMS RESOLUTION'''<br />
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{{Structure
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|PDB= 5a3h |SIZE=350|CAPTION= <scene name='initialview01'>5a3h</scene>, resolution 1.82&Aring;
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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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|LIGAND= <scene name='pdbligand=FFC:2-DEOXY-2-FLUORO-B-D-CELLOBIOSIDE'>FFC</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''2-DEOXY-2-FLURO-B-D-CELLOBIOSYL/ENZYME INTERMEDIATE COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHEARANS AT 1.8 ANGSTROMS RESOLUTION'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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5A3H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_agaradhaerens Bacillus agaradhaerens] with <scene name='pdbligand=FFC:'>FFC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Known structural/functional Sites: <scene name='pdbsite=ACI:Catalytic+Acid/Base'>ACI</scene> and <scene name='pdbsite=NUC:Catalytic+Nucleophile'>NUC</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A3H OCA].
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5A3H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_agaradhaerens Bacillus agaradhaerens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A3H OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9718293 9718293]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9718293 9718293]
[[Category: Bacillus agaradhaerens]]
[[Category: Bacillus agaradhaerens]]
[[Category: Cellulase]]
[[Category: Cellulase]]
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[[Category: skew-boat]]
[[Category: skew-boat]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:14:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:11:27 2008''

Revision as of 17:11, 20 March 2008

Image:5a3h.gif


PDB ID 5a3h

Drag the structure with the mouse to rotate
, resolution 1.82Å
Sites: and
Ligands:
Activity: Cellulase, with EC number 3.2.1.4
Coordinates: save as pdb, mmCIF, xml



2-DEOXY-2-FLURO-B-D-CELLOBIOSYL/ENZYME INTERMEDIATE COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHEARANS AT 1.8 ANGSTROMS 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

5A3H 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 Thu Mar 20 19:11:27 2008

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