From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1a3h.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1a3h.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1a3h| PDB=1a3h | SCENE= }} | | {{STRUCTURE_1a3h| PDB=1a3h | SCENE= }} |
| | | | |
| - | '''ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHERANS AT 1.6A RESOLUTION'''
| + | ===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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_9485319}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9485319 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_9485319}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 31: |
Line 35: |
| | [[Category: Glycoside hydrolase family 5]] | | [[Category: Glycoside hydrolase family 5]] |
| | [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:45:25 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:55:38 2008'' |
Revision as of 12:55, 30 June 2008
Template:STRUCTURE 1a3h
ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHERANS AT 1.6A RESOLUTION
Template:ABSTRACT PUBMED 9485319
About this Structure
1A3H 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
Page seeded by OCA on Mon Jun 30 15:55:38 2008
