1a3h

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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Andersen, K.]]
[[Category: Andersen, K.]]
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[[Category: Brzozowski, A.M.]]
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[[Category: Brzozowski, A M.]]
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[[Category: Davies, G.J.]]
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[[Category: Davies, G J.]]
[[Category: Schulein, M.]]
[[Category: Schulein, M.]]
[[Category: cellulose degradation]]
[[Category: cellulose degradation]]
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:28:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:40:30 2008''

Revision as of 09:40, 21 February 2008


1a3h, resolution 1.57Å

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ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHERANS AT 1.6A 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

1A3H is a Single protein structure of sequence from Bacillus agaradhaerens. 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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