1D3C
MICHAELIS COMPLEX OF BACILLUS CIRCULANS STRAIN 251 CYCLODEXTRIN GLYCOSYLTRANSFERASE WITH GAMMA-CYCLODEXTRIN
Summary for 1D3C
| Entry DOI | 10.2210/pdb1d3c/pdb |
| Related | 1CDG 1CXF 1CXI 1CXK 1CXL 2DIJ |
| Related PRD ID | PRD_900001 PRD_900042 |
| Descriptor | CYCLODEXTRIN GLYCOSYLTRANSFERASE, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, Cyclooctakis-(1-4)-(alpha-D-glucopyranose), ... (6 entities in total) |
| Functional Keywords | alpha-amylase, product complex, oligosaccharide, family 13 glycosyl hydrolase, transglycosylation, induced fit, catalysis, transferase |
| Biological source | Bacillus circulans |
| Total number of polymer chains | 1 |
| Total formula weight | 79099.65 |
| Authors | Uitdehaag, J.C.M.,Kalk, K.H.,van der Veen, B.A.,Dijkhuizen, L.,Dijkstra, B.W. (deposition date: 1999-09-29, release date: 1999-12-22, Last modification date: 2024-10-16) |
| Primary citation | Uitdehaag, J.C.,Kalk, K.H.,van Der Veen, B.A.,Dijkhuizen, L.,Dijkstra, B.W. The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-A resolution. J.Biol.Chem., 274:34868-34876, 1999 Cited by PubMed Abstract: The enzyme cyclodextrin glycosyltransferase is closely related to alpha-amylases but has the unique ability to produce cyclodextrins (circular alpha(1-->4)-linked glucoses) from starch. To characterize this specificity we determined a 1.8-A structure of an E257Q/D229N mutant cyclodextrin glycosyltransferase in complex with its product gamma-cyclodextrin, which reveals for the first time how cyclodextrin is competently bound. Across subsites -2, -1, and +1, the cyclodextrin ring binds in a twisted mode similar to linear sugars, giving rise to deformation of its circular symmetry. At subsites -3 and +2, the cyclodextrin binds in a manner different from linear sugars. Sequence comparisons and site-directed mutagenesis experiments support the conclusion that subsites -3 and +2 confer the cyclization activity in addition to subsite -6 and Tyr-195. On this basis, a role of the individual residues during the cyclization reaction cycle is proposed. PubMed: 10574960DOI: 10.1074/jbc.274.49.34868 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.78 Å) |
Structure validation
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