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| - | [[Image:1s2n.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1s2n| PDB=1s2n | SCENE= }} | | {{STRUCTURE_1s2n| PDB=1s2n | SCENE= }} |
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| - | '''Crystal strucure of a cold adapted subtilisin-like serine proteinase'''
| + | ===Crystal strucure of a cold adapted subtilisin-like serine proteinase=== |
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| - | ==Overview==
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| - | The crystal structure of a subtilisin-like serine proteinase from the psychrotrophic marine bacterium, Vibrio sp. PA-44, was solved by means of molecular replacement and refined at 1.84 A. This is the first structure of a cold-adapted subtilase to be determined and its elucidation facilitates examination of the molecular principles underlying temperature adaptation in enzymes. The cold-adapted Vibrio proteinase was compared with known three-dimensional structures of homologous enzymes of meso- and thermophilic origin, proteinase K and thermitase, to which it has high structural resemblance. The main structural features emerging as plausible determinants of temperature adaptation in the enzymes compared involve the character of their exposed and buried surfaces, which may be related to temperature-dependent variation in the physical properties of water. Thus, the hydrophobic effect is found to play a significant role in the structural stability of the meso- and thermophile enzymes, whereas the cold-adapted enzyme has more of its apolar surface exposed. In addition, the cold-adapted Vibrio proteinase is distinguished from the more stable enzymes by its strong anionic character arising from the high occurrence of uncompensated negatively charged residues at its surface. Interestingly, both the cold-adapted and thermophile proteinases differ from the mesophile enzyme in having more extensive hydrogen- and ion pair interactions in their structures; this supports suggestions of a dual role of electrostatic interactions in the adaptation of enzymes to both high and low temperatures. The Vibrio proteinase has three calcium ions associated with its structure, one of which is in a calcium-binding site not described in other subtilases. | + | The line below this paragraph, {{ABSTRACT_PUBMED_15670163}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15670163 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15670163}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Kristjansson, M M.]] | | [[Category: Kristjansson, M M.]] |
| | [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:13:13 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:52:49 2008'' |
Revision as of 08:52, 28 July 2008
Template:STRUCTURE 1s2n
Crystal strucure of a cold adapted subtilisin-like serine proteinase
Template:ABSTRACT PUBMED 15670163
About this Structure
1S2N is a Single protein structure of sequence from Bacteria. Full crystallographic information is available from OCA.
Reference
Crystal structure of a subtilisin-like serine proteinase from a psychrotrophic Vibrio species reveals structural aspects of cold adaptation., Arnorsdottir J, Kristjansson MM, Ficner R, FEBS J. 2005 Feb;272(3):832-45. PMID:15670163
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