2a3h: Difference between revisions
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==Overview== | ==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., ... | 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== | ||
2A3H is a | 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] Structure known Active Site: AVE. 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 Mon Nov 5 15:18:45 2007'' | ||
