1wza
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(New page: 200px<br /><applet load="1wza" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wza, resolution 1.60Å" /> '''Crystal structure of...)
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Revision as of 22:58, 24 November 2007
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Crystal structure of alpha-amylase from H.orenii
Overview
Here we report the first crystal structure of a protein, AmyA, a secretory, alpha-amylase isolated from Halothermothrix orenii, which is both, halophilic and thermophilic. The crystal structure was determined at 1.6 A, resolution. AmyA lacks the conserved acidic surface, which is considered, essential for protein stability at high salinity. Sedimentation velocity, and CD experiments on AmyA reveal the formation of unique reversible, poly-dispersed oligomers that show unusually high thermal stability. These, studies provide valuable insight into the structural elements that, contribute to the stability of AmyA at both physical and chemical extremes, and their functional implications.
About this Structure
1WZA is a Single protein structure of sequence from Halothermothrix orenii with CA as ligand. Active as Alpha-amylase, with EC number 3.2.1.1 Full crystallographic information is available from OCA.
Reference
Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition., Sivakumar N, Li N, Tang JW, Patel BK, Swaminathan K, FEBS Lett. 2006 May 15;580(11):2646-52. Epub 2006 Apr 19. PMID:16647060
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