1wza: Difference between revisions

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[[Image:1wza.gif|left|200px]]
{{Seed}}
[[Image:1wza.png|left|200px]]


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{{STRUCTURE_1wza|  PDB=1wza  |  SCENE=  }}  
{{STRUCTURE_1wza|  PDB=1wza  |  SCENE=  }}  


'''Crystal structure of alpha-amylase from H.orenii'''
===Crystal structure of alpha-amylase from H.orenii===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_16647060}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 16647060 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16647060}}


==About this Structure==
==About this Structure==
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/16647060 16647060]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16647060 16647060]
Cloning, sequencing and expression of an alpha-amylase gene, amyA, from the thermophilic halophile Halothermothrix orenii and purification and biochemical characterization of the recombinant enzyme., Mijts BN, Patel BK, Microbiology. 2002 Aug;148(Pt 8):2343-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12177328 12177328]
[[Category: Alpha-amylase]]
[[Category: Alpha-amylase]]
[[Category: Halothermothrix orenii]]
[[Category: Halothermothrix orenii]]
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Thermophilic]]
[[Category: Thermophilic]]
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