1ded
From Proteopedia
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|PDB= 1ded |SIZE=350|CAPTION= <scene name='initialview01'>1ded</scene>, resolution 2.0Å | |PDB= 1ded |SIZE=350|CAPTION= <scene name='initialview01'>1ded</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACR:ACARBOSE'>ACR</scene> | + | |LIGAND= <scene name='pdbligand=ACR:ACARBOSE'>ACR</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1d7f|1D7F]], [[1pam|1PAM]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ded FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ded OCA], [http://www.ebi.ac.uk/pdbsum/1ded PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ded RCSB]</span> | ||
}} | }} | ||
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[[Category: Ishii, N.]] | [[Category: Ishii, N.]] | ||
[[Category: Yamane, K.]] | [[Category: Yamane, K.]] | ||
| - | [[Category: ACR]] | ||
| - | [[Category: CA]] | ||
[[Category: acarbose]] | [[Category: acarbose]] | ||
[[Category: cgtase]] | [[Category: cgtase]] | ||
[[Category: cyclodextrin glucanotransferase]] | [[Category: cyclodextrin glucanotransferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:39:58 2008'' |
Revision as of 16:40, 30 March 2008
| |||||||
| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Cyclomaltodextrin glucanotransferase, with EC number 2.4.1.19 | ||||||
| Related: | 1D7F, 1PAM
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF ALKALOPHILIC ASPARAGINE 233-REPLACED CYCLODEXTRIN GLUCANOTRANSFERASE COMPLEXED WITH AN INHIBITOR, ACARBOSE, AT 2.0 A RESOLUTION
Overview
The product specificity of cyclodextrin glucanotransferase (CGTase) from alkalophilic Bacillus sp. #1011 is improved to near-uniformity by mutation of histidine-233 to asparagine. Asparagine 233-replaced CGTase (H233N-CGTase) no longer produces alpha-cyclodextrin, while the wild-type CGTase from the same bacterium produces a mixture of predominantly alpha-, beta-, and gamma-cyclodextrins, catalyzing the conversion of starch into cyclic or linear alpha-1,4-linked glucopyranosyl chains. In order to better understand the protein engineering of H233N-CGTase, the crystal structure of the mutant enzyme complexed with a maltotetraose analog, acarbose, was determined at 2.0 A resolution with a final crystallographic R value of 0.163 for all data. Taking a close look at the active site cleft in which the acarbose molecule is bound, the most probable reason for the improved specificity of H233N-CGTase is the removal of interactions needed to form a compact ring like a-cyclodextrin.
About this Structure
1DED is a Single protein structure of sequence from Bacillus sp.. Full crystallographic information is available from OCA.
Reference
Crystal structure of alkalophilic asparagine 233-replaced cyclodextrin glucanotransferase complexed with an inhibitor, acarbose, at 2.0 A resolution., Ishii N, Haga K, Yamane K, Harata K, J Biochem. 2000 Mar;127(3):383-91. PMID:10731709
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