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 1.60&Aring;" /> '''Crystal structure of...)
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[[Image:1wza.gif|left|200px]]<br /><applet load="1wza" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1wza.gif|left|200px]]<br /><applet load="1wza" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1wza, resolution 1.60&Aring;" />
caption="1wza, resolution 1.60&Aring;" />
'''Crystal structure of alpha-amylase from H.orenii'''<br />
'''Crystal structure of alpha-amylase from H.orenii'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1WZA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halothermothrix_orenii Halothermothrix orenii] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WZA OCA].
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1WZA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halothermothrix_orenii Halothermothrix orenii] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZA OCA].
==Reference==
==Reference==
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[[Category: thermophilic]]
[[Category: thermophilic]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:06:26 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:49:36 2008''

Revision as of 13:49, 21 February 2008


1wza, resolution 1.60Å

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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 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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