1g1y
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=BCD:BETA-CYCLODEXTRIN'>BCD</scene> | |LIGAND= <scene name='pdbligand=BCD:BETA-CYCLODEXTRIN'>BCD</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Neopullulanase Neopullulanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.135 3.2.1.135] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Neopullulanase Neopullulanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.135 3.2.1.135] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1y OCA], [http://www.ebi.ac.uk/pdbsum/1g1y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g1y RCSB]</span> | ||
}} | }} | ||
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[[Category: Sakano, Y.]] | [[Category: Sakano, Y.]] | ||
[[Category: Tonozuka, T.]] | [[Category: Tonozuka, T.]] | ||
| - | [[Category: BCD]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''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 20:34:50 2008'' |
Revision as of 17:34, 30 March 2008
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| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Neopullulanase, with EC number 3.2.1.135 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF ALPHA-AMYLASE II (TVAII) FROM THERMOACTINOMYCES VULGARIS R-47 AND BETA-CYCLODEXTRIN COMPLEX
Overview
Crystals of the mutant E354A of Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII) complexed with beta-cyclodextrin were prepared by a soaking method, and the diffraction data were collected at 100 K, using Synchrotron radiation (SPring-8). The crystals belong to an orthorhombic system with the space group P2(1)2(1)2(1) and cell dimensions a = 111.1 A, b = 117.7 A, c = 113.3 A, which is almost isomorphous with crystals of the wild-type TVAII, and the structure was refined to an R-factor = 0.208 (R(free) = 0.252) using 3.0 A resolution data. The refined structure shows that the interactions between Phe286 and two C6 atoms of beta-cyclodextrin at the hydrolyzing site are important for TVAII to recognize cyclodextrins as substrates. This observation from the X-ray structure was supported by kinetic analyses of cyclodextrins using the wild-type TVAII, the mutant F286A and F286L. These studies also suggested that the TVAII-hydrolyzing mechanism for cyclodextrins is slightly different from that for starch.
About this Structure
1G1Y is a Single protein structure of sequence from Thermoactinomyces vulgaris. Full crystallographic information is available from OCA.
Reference
Studies on the hydrolyzing mechanism for cyclodextrins of Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII). X-ray structure of the mutant E354A complexed with beta-cyclodextrin, and kinetic analyses on cyclodextrins., Kondo S, Ohtaki A, Tonozuka T, Sakano Y, Kamitori S, J Biochem. 2001 Mar;129(3):423-8. PMID:11226882
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