1PJ9
Bacillus circulans strain 251 loop mutant 183-195
Summary for 1PJ9
| Entry DOI | 10.2210/pdb1pj9/pdb |
| Related | 1CDG |
| Related PRD ID | PRD_900001 PRD_900009 |
| Descriptor | Cyclomaltodextrin glucanotransferase, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (8 entities in total) |
| Functional Keywords | glycosyltransferase, transferase, cyclodextrin |
| Biological source | Bacillus circulans |
| Total number of polymer chains | 1 |
| Total formula weight | 77283.95 |
| Authors | Rozeboom, H.J.,Dijkstra, B.W. (deposition date: 2003-06-02, release date: 2004-02-03, Last modification date: 2024-11-06) |
| Primary citation | Leemhuis, H.,Rozeboom, H.J.,Dijkstra, B.W.,Dijkhuizen, L. Improved thermostability of bacillus circulans cyclodextrin glycosyltransferase by the introduction of a salt bridge PROTEINS: STRUCT.,FUNCT.,GENET., 54:128-134, 2004 Cited by PubMed Abstract: 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. PubMed: 14705029DOI: 10.1002/prot.10516 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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