2a3h
From Proteopedia
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| - | [[Image:2a3h.gif|left|200px]]<br /> | + | [[Image:2a3h.gif|left|200px]]<br /><applet load="2a3h" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2a3h" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="2a3h, resolution 2.0Å" /> | caption="2a3h, resolution 2.0Å" /> | ||
'''CELLOBIOSE COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHERANS AT 2.0 A RESOLUTION'''<br /> | '''CELLOBIOSE COMPLEX OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHERANS AT 2.0 A RESOLUTION'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2A3H 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 CBI 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] | + | 2A3H 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 CBI 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 Site: <scene name='pdbsite=AVE:Ave Site'>AVE</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2A3H OCA]. |
==Reference== | ==Reference== | ||
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[[Category: glycoside hydrolase family 5]] | [[Category: glycoside hydrolase family 5]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:42:51 2007'' |
Revision as of 16:33, 18 December 2007
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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 with CBI as ligand. Active as Cellulase, with EC number 3.2.1.4 Known structural/functional Site: . 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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