Structural highlights
Function
Q33E90_9BACI
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of the GH13 alpha-glucosidase (GSJ) from deep-sea bacterium Geobacillus sp. strain HTA-462 was determined to a 2.0 A resolution. Comparisons of the GSJ structure with that of other GH13 enzymes with different catalytic activities revealed that the catalytic cleft of GSJ was widely opened when compared with the homologues. The wide opening of the catalytic cleft originated from conformational changes of active site residues and disorder of the regions close to the catalytic center. This structural feature of GSJ would explain the ability of this enzyme to accept a wide variety of nonsugar molecules as acceptors in the transglycosylation reaction.
Crystal structure of GH13 alpha-glucosidase GSJ from one of the deepest sea bacteria.,Shirai T, Hung VS, Morinaka K, Kobayashi T, Ito S Proteins. 2008 Oct;73(1):126-33. PMID:18398906[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shirai T, Hung VS, Morinaka K, Kobayashi T, Ito S. Crystal structure of GH13 alpha-glucosidase GSJ from one of the deepest sea bacteria. Proteins. 2008 Oct;73(1):126-33. PMID:18398906 doi:10.1002/prot.22044