1pj9
From Proteopedia
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Bacillus circulans strain 251 loop mutant 183-195
Overview
Cyclodextrin glycosyltransferase (CGTase) catalyzes the formation of, cyclodextrins from starch. Among the CGTases with known three-dimensional, structure, Thermoanaerobacterium thermosulfurigenes CGTase has the highest, thermostability. By replacing amino acid residues in the B-domain of, Bacillus circulans CGTase with those from T. thermosulfurigenes CGTase, we, identified a B. circulans CGTase mutant (with N188D and K192R mutations), with a strongly increased activity half-life at 60 degrees C. Asp188 and, Arg192 form a salt bridge in T. thermosulfurigenes CGTase. Structural, analysis of the B. circulans CGTase mutant revealed that this salt bridge, is also formed in the mutant. Thus, the activity half-life of this enzyme, can be enhanced by rational protein engineering.
About this Structure
1PJ9 is a Single protein structure of sequence from Bacillus circulans with MAL, GLC, CA, MPD and ACY as ligands. Active as Cyclomaltodextrin glucanotransferase, with EC number 2.4.1.19 Full crystallographic information is available from OCA.
Reference
Improved thermostability of bacillus circulans cyclodextrin glycosyltransferase by the introduction of a salt bridge., Leemhuis H, Rozeboom HJ, Dijkstra BW, Dijkhuizen L, Proteins. 2004 Jan 1;54(1):128-34. PMID:14705029
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