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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"
caption="1wsd, resolution 1.5&Aring;" />
'''Alkaline M-protease form I crystal strcuture'''<br />


==Overview==
==Alkaline M-protease form I crystal structure==
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.
<StructureSection load='1wsd' size='340' side='right'caption='[[1wsd]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1wsd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_clausii_KSM-K16 Alkalihalobacillus clausii KSM-K16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WSD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WSD FirstGlance]. <br>
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WSD OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wsd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wsd OCA], [https://pdbe.org/1wsd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wsd RCSB], [https://www.ebi.ac.uk/pdbsum/1wsd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wsd ProSAT]</span></td></tr>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9278275 9278275]
</table>
[[Category: Bacillus sp.]]
== Function ==
[[Category: Single protein]]
[https://www.uniprot.org/uniprot/PRTM_ALKCK PRTM_ALKCK] Alkaline serine protease that cleaves various substrates, including N-succinyl-Ala-Ala-Pro-Phe-pNA, N-succinyl-Ala-Ala-Pro-MetpNA, oxidized insulin B chain, casein, hemoglobin and scleroproteins, such as keratin, alpha-keratin and elastin.<ref>PMID:7632397</ref>
[[Category: Ashida, T.]]
== Evolutionary Conservation ==
[[Category: Hitomi, J.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Ito, S.]]
Check<jmol>
[[Category: Kobayashi, T.]]
  <jmolCheckbox>
[[Category: Shirai, T.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ws/1wsd_consurf.spt"</scriptWhenChecked>
[[Category: Suzuki, A.]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: Yamane, T.]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: CA]]
  </jmolCheckbox>
[[Category: SO4]]
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wsd ConSurf].
[[Category: detergent enzyme]]
<div style="clear:both"></div>
[[Category: high-alkaline]]
== References ==
[[Category: subtilisin]]
<references/>
 
__TOC__
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:38:40 2007''
</StructureSection>
[[Category: Alkalihalobacillus clausii KSM-K16]]
[[Category: Large Structures]]
[[Category: Ashida T]]
[[Category: Hitomi J]]
[[Category: Ito S]]
[[Category: Kobayashi T]]
[[Category: Shirai T]]
[[Category: Suzuki A]]
[[Category: Yamane T]]

Latest revision as of 13:33, 13 March 2024

Alkaline M-protease form I crystal structure

1wsd, resolution 1.50Å

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