2a3h
From Proteopedia
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|SITE= <scene name='pdbsite=AVE:Ave+Site'>AVE</scene> | |SITE= <scene name='pdbsite=AVE:Ave+Site'>AVE</scene> | ||
|LIGAND= <scene name='pdbligand=CBI:CELLOBIOSE'>CBI</scene> | |LIGAND= <scene name='pdbligand=CBI:CELLOBIOSE'>CBI</scene> | ||
| - | |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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a3h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a3h OCA], [http://www.ebi.ac.uk/pdbsum/2a3h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2a3h RCSB]</span> | ||
}} | }} | ||
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[[Category: Davies, G J.]] | [[Category: Davies, G J.]] | ||
[[Category: Schulein, M.]] | [[Category: Schulein, M.]] | ||
| - | [[Category: CBI]] | ||
[[Category: cellulose degradation]] | [[Category: cellulose degradation]] | ||
[[Category: endoglucanase]] | [[Category: endoglucanase]] | ||
[[Category: glycoside hydrolase family 5]] | [[Category: glycoside hydrolase family 5]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:47:20 2008'' |
Revision as of 22:47, 30 March 2008
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| , resolution 2.0Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Cellulase, with EC number 3.2.1.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CELLOBIOSE COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHERANS AT 2.0 A RESOLUTION
Overview
The enzymatic degradation of cellulose, by cellulases, is not only industrially important in the food, paper, and textile industries but also a potentially useful method for the environmentally friendly recycling of municipal waste. An understanding of the structural and mechanistic requirements for the hydrolysis of the beta-1,4 glycosidic bonds of cellulose is an essential prerequisite for beneficial engineering of cellulases for these processes. Cellulases have been classified into 13 of the 62 glycoside hydrolase families [Henrissat, B., and Bairoch, A. (1996) Biochem J. 316, 695-696]. The structure of the catalytic core of the family 5 endoglucanase, Ce15A, from the alkalophilic Bacillus agaradherans has been solved by multiple isomorphous replacement at 1.6 A resolution. Ce15A has the (alpha/beta)8 barrel structure and signature structural features typical of the grouping of glycoside hydrolase families known as clan GH-A, with the catalytic acid/base Glu 139 and nucleophile Glu 228 on barrel strands beta 4 and beta 7 as expected. In addition to the native enzyme, the 2.0 A resolution structure of the cellobiose-bound form of the enzyme has also been determined. Cellobiose binds preferentially in the -2 and -3 subsites of the enzyme. Kinetic studies on the isolated catalytic core domain of Ce15A, using a series of reduced cellodextrins as substrates, suggest approximately five to six binding sites, consistent with the shape and size of the cleft observed by crystallography.
About this Structure
2A3H is a Single protein structure of sequence from Bacillus agaradhaerens. Full crystallographic information is available from OCA.
Reference
Structure of the Bacillus agaradherans family 5 endoglucanase at 1.6 A and its cellobiose complex at 2.0 A resolution., Davies GJ, Dauter M, Brzozowski AM, Bjornvad ME, Andersen KV, Schulein M, Biochemistry. 1998 Feb 17;37(7):1926-32. PMID:9485319
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