1ji2: Difference between revisions

Revision as of 20:16, 1 July 2008

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File:1ji2.png

Template:STRUCTURE 1ji2

Improved X-ray Structure of Thermoactinomyces vulgaris R-47 alpha-Amylase 2Improved X-ray Structure of Thermoactinomyces vulgaris R-47 alpha-Amylase 2

Template:ABSTRACT PUBMED 12051850

About this StructureAbout this Structure

1JI2 is a Single protein structure of sequence from Thermoactinomyces vulgaris. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures and structural comparison of Thermoactinomyces vulgaris R-47 alpha-amylase 1 (TVAI) at 1.6 A resolution and alpha-amylase 2 (TVAII) at 2.3 A resolution., Kamitori S, Abe A, Ohtaki A, Kaji A, Tonozuka T, Sakano Y, J Mol Biol. 2002 Apr 26;318(2):443-53. PMID:12051850

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Improved X-ray Structure of Thermoactinomyces vulgaris R-47 alpha-Amylase 2'''
+===Improved X-ray Structure of Thermoactinomyces vulgaris R-47 alpha-Amylase 2===
-==Overview==
+<!--
-The X-ray crystal structures of Thermoactinomyces vulgaris R-47 alpha-amylase 1 (TVAI) and alpha-amylase 2 (TVAII) have been determined at 1.6 A and 2.3 A resolution, respectively. The structures of TVAI and TVAII have been refined, R-factor of 0.182 (R(free)=0.206) and 0.179 (0.224), respectively, with good chemical geometries. Both TVAI and TVAII have four domains, N, A, B and C, and all very similar in structure. However, there are some differences in the structures between them. Domain N of TVAI interacts strongly with domains A and B, giving a spherical shape structure to the enzyme, while domain N of TVAII is isolated from the other domains, which leads to the formation of a dimer. TVAI has three bound Ca ions, whereas TVAII has only one. TVAI has eight extra loops compared to TVAII, while TVAII has two extra loops compared to TVAI. TVAI can hydrolyze substrates more efficiently than TVAII with a high molecular mass such as starch, while TVAII is much more active against cyclodextrins than TVAI and other alpha-amylases. A structural comparison of the active sites has clearly revealed this difference in substrate specificity.
+The line below this paragraph, {{ABSTRACT_PUBMED_12051850}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12051850}}
 ==About this Structure==
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 [[Category: Tonozuka, T.]]
 [[Category: Beta/alpha barrel]]
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