1wsd
From Proteopedia
(New page: 200px<br /><applet load="1wsd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wsd, resolution 1.5Å" /> '''Alkaline M-protease f...) |
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| - | [[Image:1wsd.jpg|left|200px]]<br /><applet load="1wsd" size=" | + | [[Image:1wsd.jpg|left|200px]]<br /><applet load="1wsd" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wsd, resolution 1.5Å" /> | caption="1wsd, resolution 1.5Å" /> | ||
'''Alkaline M-protease form I crystal strcuture'''<br /> | '''Alkaline M-protease form I crystal strcuture'''<br /> | ||
==Overview== | ==Overview== | ||
| - | M-protease is a subtilisin-family serine protease produced by an | + | M-protease is a subtilisin-family serine protease produced by an alkaliphilic Bacillus sp. strain. Optimal enzymatic activity of the protein occurs at pH 12.3. The crystal structure of M-protease (space group P2(1)2(1)2(1), a = 62.3, b = 75.5, c = 47.2 A) has been refined to a crystallographic R-factor of 17.2% at 1.5 A resolution. The alkaline adaptation mechanism of the enzyme was analyzed. Molecular phylogeny construction was used to determine the amino acid substitutions that occurred during the high-alkaline adaptation process. This analysis revealed a decrease in the number of negatively charged amino acids (aspartic acid and glutamic acid) and lysine residues and an increase in arginine and neutral hydrophilic amino acids (histidine, asparagine and glutamine) residues during the course of adaptation. These substitutions increased the isoelectric point of M-protease. Some of the acquired arginine residues form hydrogen bonds or ion pairs to combine both N- and C-terminal regions of M-protease. The substituted residues are localized to a hemisphere of the globular protein molecule where positional shifts of peptide segments, relative to those of the less alkaliphilic subtilisin Carlsberg, are observed. The biased distribution and interactions caused by the substituted residues seem to be responsible for stabilization of the conformation in a high-alkaline condition. |
==About this Structure== | ==About this Structure== | ||
| - | 1WSD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.] with CA and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1WSD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WSD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: subtilisin]] | [[Category: subtilisin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:47:41 2008'' |
Revision as of 13:47, 21 February 2008
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Alkaline M-protease form I crystal strcuture
Overview
M-protease is a subtilisin-family serine protease produced by an alkaliphilic Bacillus sp. strain. Optimal enzymatic activity of the protein occurs at pH 12.3. The crystal structure of M-protease (space group P2(1)2(1)2(1), a = 62.3, b = 75.5, c = 47.2 A) has been refined to a crystallographic R-factor of 17.2% at 1.5 A resolution. The alkaline adaptation mechanism of the enzyme was analyzed. Molecular phylogeny construction was used to determine the amino acid substitutions that occurred during the high-alkaline adaptation process. This analysis revealed a decrease in the number of negatively charged amino acids (aspartic acid and glutamic acid) and lysine residues and an increase in arginine and neutral hydrophilic amino acids (histidine, asparagine and glutamine) residues during the course of adaptation. These substitutions increased the isoelectric point of M-protease. Some of the acquired arginine residues form hydrogen bonds or ion pairs to combine both N- and C-terminal regions of M-protease. The substituted residues are localized to a hemisphere of the globular protein molecule where positional shifts of peptide segments, relative to those of the less alkaliphilic subtilisin Carlsberg, are observed. The biased distribution and interactions caused by the substituted residues seem to be responsible for stabilization of the conformation in a high-alkaline condition.
About this Structure
1WSD is a Single protein structure of sequence from Bacillus sp. with and as ligands. Full crystallographic information is available from OCA.
Reference
High-resolution crystal structure of M-protease: phylogeny aided analysis of the high-alkaline adaptation mechanism., Shirai T, Suzuki A, Yamane T, Ashida T, Kobayashi T, Hitomi J, Ito S, Protein Eng. 1997 Jun;10(6):627-34. PMID:9278275
Page seeded by OCA on Thu Feb 21 15:47:41 2008
Categories: Bacillus sp. | Single protein | Ashida, T. | Hitomi, J. | Ito, S. | Kobayashi, T. | Shirai, T. | Suzuki, A. | Yamane, T. | CA | SO4 | Detergent enzyme | High-alkaline | Subtilisin
