1g1y

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[[Image:1g1y.gif|left|200px]]<br /><applet load="1g1y" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1g1y.gif|left|200px]]
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caption="1g1y, resolution 3.0&Aring;" />
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'''CRYSTAL STRUCTURE OF ALPHA-AMYLASE II (TVAII) FROM THERMOACTINOMYCES VULGARIS R-47 AND BETA-CYCLODEXTRIN COMPLEX'''<br />
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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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|SITE=
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|LIGAND= <scene name='pdbligand=BCD:BETA-CYCLODEXTRIN'>BCD</scene>
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|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]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF ALPHA-AMYLASE II (TVAII) FROM THERMOACTINOMYCES VULGARIS R-47 AND BETA-CYCLODEXTRIN COMPLEX'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1G1Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris] with <scene name='pdbligand=BCD:'>BCD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1Y OCA].
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1G1Y is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1Y OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11226882 11226882]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11226882 11226882]
[[Category: Neopullulanase]]
[[Category: Neopullulanase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:45:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:17:03 2008''

Revision as of 09:17, 20 March 2008


PDB ID 1g1y

Drag the structure with the mouse to rotate
, resolution 3.0Å
Ligands:
Activity: Neopullulanase, with EC number 3.2.1.135
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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