2die

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Revision as of 17:03, 29 January 2008

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spinqualitylabelsall models 2die, resolution 2.1Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Alkaline alpha-amylase AmyK from Bacillus sp. KSM-1378

Overview

The crystal structure of alkaline liquefying alpha-amylase (AmyK) from the, alkaliphilic Bacillus sp. KSM-1378 was determined at 2.1 A resolution. The, AmyK structure belongs to the GH13 glycoside hydrolase family, which, consists of three domains, and bound three calcium and one sodium ions., The alkaline adaptation mechanism of AmyK was investigated by the, ancestral sequence evolutionary trace method and by extensive comparisons, between alkaline and nonalkaline enzyme structures, including three other, protein families: protease, cellulase, and phosphoserine aminotransferase., The consensus change for the alkaline adaptation process was a decrease in, the Lys content. The loss of a Lys residue is associated with ion pair, remodeling, which mainly consists of the loss of Lys-Asp/Glu ion pairs and, the acquisition of Arg ion pairs, preferably Arg-Glu. The predicted, replacements of the positively charged amino acids were often, although, not always, used for ion pair remodeling.

About this Structure

2DIE is a Single protein structure of sequence from Bacillus sp. with and as ligands. Full crystallographic information is available from OCA.

Reference

Ancestral sequence evolutionary trace and crystal structure analyses of alkaline alpha-amylase from Bacillus sp. KSM-1378 to clarify the alkaline adaptation process of proteins., Shirai T, Igarashi K, Ozawa T, Hagihara H, Kobayashi T, Ozaki K, Ito S, Proteins. 2007 Feb 15;66(3):600-10. PMID:17154418

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