1wza
From Proteopedia
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| - | [[Image:1wza.gif|left|200px]] | + | [[Image:1wza.gif|left|200px]] |
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| - | '''Crystal structure of alpha-amylase from H.orenii''' | + | {{Structure |
| + | |PDB= 1wza |SIZE=350|CAPTION= <scene name='initialview01'>1wza</scene>, resolution 1.60Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= AMYA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=31909 Halothermothrix orenii]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of alpha-amylase from H.orenii''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1WZA is a [ | + | 1WZA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Halothermothrix_orenii Halothermothrix orenii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZA OCA]. |
==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:// | + | 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] |
[[Category: Alpha-amylase]] | [[Category: Alpha-amylase]] | ||
[[Category: Halothermothrix orenii]] | [[Category: Halothermothrix orenii]] | ||
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[[Category: thermophilic]] | [[Category: thermophilic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:03:23 2008'' |
Revision as of 13:03, 20 March 2008
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| , resolution 1.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | AMYA (Halothermothrix orenii) | ||||||
| Activity: | Alpha-amylase, with EC number 3.2.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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