1sh7: Difference between revisions

Revision as of 16:01, 21 February 2008

Crystal structure of a cold adapted subtilisin-like serine proteinase

OverviewOverview

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.

About this StructureAbout this Structure

1SH7 is a Single protein structure of sequence from Vibrio sp. pa-44 with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

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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-[[Image:1sh7.gif|left|200px]]<br /><applet load="1sh7" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1sh7.gif|left|200px]]<br /><applet load="1sh7" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1sh7, resolution 1.84&Aring;" />
 '''Crystal structure of a cold adapted subtilisin-like serine proteinase'''<br />
 ==Overview==
-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 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.
 ==About this Structure==
-SH7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_sp._pa-44 Vibrio sp. pa-44] with CA and PMS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SH7 OCA].
+SH7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_sp._pa-44 Vibrio sp. pa-44] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=PMS:'>PMS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SH7 OCA].
 ==Reference==
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 [[Category: Arnorsdottir, J.]]
 [[Category: Ficner, R.]]
-[[Category: Kristjansson, M.M.]]
+[[Category: Kristjansson, M M.]]
 [[Category: CA]]
 [[Category: PMS]]
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 [[Category: subtilisin-like proteinase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:29:46 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:01:27 2008''