1d3c
From Proteopedia
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- | [[Image:1d3c.gif|left|200px]] | + | [[Image:1d3c.gif|left|200px]] |
- | + | ||
- | '''MICHAELIS COMPLEX OF BACILLUS CIRCULANS STRAIN 251 CYCLODEXTRIN GLYCOSYLTRANSFERASE WITH GAMMA-CYCLODEXTRIN''' | + | {{Structure |
+ | |PDB= 1d3c |SIZE=350|CAPTION= <scene name='initialview01'>1d3c</scene>, resolution 1.78Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene> | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Cyclomaltodextrin_glucanotransferase Cyclomaltodextrin glucanotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.19 2.4.1.19] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''MICHAELIS COMPLEX OF BACILLUS CIRCULANS STRAIN 251 CYCLODEXTRIN GLYCOSYLTRANSFERASE WITH GAMMA-CYCLODEXTRIN''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1D3C is a [ | + | 1D3C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_circulans Bacillus circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D3C OCA]. |
==Reference== | ==Reference== | ||
- | The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-A resolution., Uitdehaag JC, Kalk KH, van Der Veen BA, Dijkhuizen L, Dijkstra BW, J Biol Chem. 1999 Dec 3;274(49):34868-76. PMID:[http:// | + | The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-A resolution., Uitdehaag JC, Kalk KH, van Der Veen BA, Dijkhuizen L, Dijkstra BW, J Biol Chem. 1999 Dec 3;274(49):34868-76. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10574960 10574960] |
[[Category: Bacillus circulans]] | [[Category: Bacillus circulans]] | ||
[[Category: Cyclomaltodextrin glucanotransferase]] | [[Category: Cyclomaltodextrin glucanotransferase]] | ||
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[[Category: transglycosylation]] | [[Category: transglycosylation]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:32:18 2008'' |
Revision as of 08:32, 20 March 2008
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, resolution 1.78Å | |||||||
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Ligands: | and | ||||||
Activity: | Cyclomaltodextrin glucanotransferase, with EC number 2.4.1.19 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
MICHAELIS COMPLEX OF BACILLUS CIRCULANS STRAIN 251 CYCLODEXTRIN GLYCOSYLTRANSFERASE WITH GAMMA-CYCLODEXTRIN
Overview
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.
About this Structure
1D3C is a Single protein structure of sequence from Bacillus circulans. Full crystallographic information is available from OCA.
Reference
The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-A resolution., Uitdehaag JC, Kalk KH, van Der Veen BA, Dijkhuizen L, Dijkstra BW, J Biol Chem. 1999 Dec 3;274(49):34868-76. PMID:10574960
Page seeded by OCA on Thu Mar 20 10:32:18 2008
Categories: Bacillus circulans | Cyclomaltodextrin glucanotransferase | Single protein | Dijkhuizen, L. | Dijkstra, B W. | Kalk, K H. | Uitdehaag, J C.M. | Veen, B A.van der. | CA | MPD | Alpha-amylase | Catalysis | Family 13 glycosyl hydrolase | Induced fit | Oligosaccharide | Product complex | Transglycosylation