1g1y

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[[Image:1g1y.gif|left|200px]]
[[Image:1g1y.gif|left|200px]]
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{{Structure
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|PDB= 1g1y |SIZE=350|CAPTION= <scene name='initialview01'>1g1y</scene>, resolution 3.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1g1y", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=BCD:BETA-CYCLODEXTRIN'>BCD</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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{{STRUCTURE_1g1y| PDB=1g1y | SCENE= }}
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|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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'''CRYSTAL STRUCTURE OF ALPHA-AMYLASE II (TVAII) FROM THERMOACTINOMYCES VULGARIS R-47 AND BETA-CYCLODEXTRIN COMPLEX'''
'''CRYSTAL STRUCTURE OF ALPHA-AMYLASE II (TVAII) FROM THERMOACTINOMYCES VULGARIS R-47 AND BETA-CYCLODEXTRIN COMPLEX'''
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[[Category: Sakano, Y.]]
[[Category: Sakano, Y.]]
[[Category: Tonozuka, T.]]
[[Category: Tonozuka, T.]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:02:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:34:50 2008''
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Revision as of 14:02, 2 May 2008

Image:1g1y.gif

Template:STRUCTURE 1g1y

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 Page seeded by OCA on Fri May 2 17:02:01 2008

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