1ht6
From Proteopedia
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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
Page seeded by OCA on Tue Nov 20 16:48:50 2007
Categories: Alpha-amylase | Hordeum vulgare | Single protein | Aghajari, N. | Haser, R. | Robert, X. | CA | EDO | Barley | Beta-alpha-barrel | Isozyme 1
