1ht6

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(New page: 200px<br /><applet load="1ht6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ht6, resolution 1.50&Aring;" /> '''CRYSTAL STRUCTURE AT...)
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Revision as of 14:41, 20 November 2007

Image:1ht6.jpg

1ht6, resolution 1.50Å

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CRYSTAL STRUCTURE AT 1.5A RESOLUTION OF THE BARLEY ALPHA-AMYLASE ISOZYME 1

Overview

Though the three-dimensional structures of barley alpha-amylase isozymes, AMY1 and AMY2 are very similar, they differ remarkably from each other in, their affinity for Ca(2+) and when interacting with substrate analogs. A, surface site recognizing maltooligosaccharides, not earlier reported for, other alpha-amylases and probably associated with the different activity, of AMY1 and AMY2 toward starch granules, has been identified. It is, located in the C-terminal part of the enzyme and, thus, highlights a, potential role of domain C. In order to scrutinize the possible biological, significance of this domain in alpha-amylases, a thorough comparison of, their three-dimensional structures was conducted. An additional role for, an earlier-identified starch granule binding surface site is proposed, and, a new calcium ion is reported.

About this Structure

1HT6 is a Single protein structure of sequence from Hordeum vulgare with CA and EDO as ligands. Active as Alpha-amylase, with EC number 3.2.1.1 Full crystallographic information is available from OCA.

Reference

The structure of barley alpha-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding: a pair of sugar tongs., Robert X, Haser R, Gottschalk TE, Ratajczak F, Driguez H, Svensson B, Aghajari N, Structure. 2003 Aug;11(8):973-84. PMID:12906828

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