1A3H
ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHERANS AT 1.6A RESOLUTION
Summary for 1A3H
| Entry DOI | 10.2210/pdb1a3h/pdb |
| Descriptor | ENDOGLUCANASE (2 entities in total) |
| Functional Keywords | hydrolase, cellulose degradation, endoglucanase, glycoside hydrolase family 5 |
| Biological source | Bacillus agaradhaerens |
| Cellular location | Secreted : O85465 |
| Total number of polymer chains | 1 |
| Total formula weight | 33653.75 |
| Authors | Davies, G.J.,Brzozowski, A.M.,Andersen, K.,Schulein, M. (deposition date: 1998-01-21, release date: 1999-03-16, Last modification date: 2024-02-07) |
| Primary citation | Davies, G.J.,Dauter, M.,Brzozowski, A.M.,Bjornvad, M.E.,Andersen, K.V.,Schulein, M. Structure of the Bacillus agaradherans family 5 endoglucanase at 1.6 A and its cellobiose complex at 2.0 A resolution Biochemistry, 37:1926-1932, 1998 Cited by PubMed Abstract: 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. PubMed: 9485319DOI: 10.1021/bi972162m PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.57 Å) |
Structure validation
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