View source for 2wv7


==Intracellular subtilisin precursor from B. clausii==
<StructureSection load='2wv7' size='340' side='right'caption='[[2wv7]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2wv7]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_clausii Alkalihalobacillus clausii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WV7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WV7 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wv7 OCA], [https://pdbe.org/2wv7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wv7 RCSB], [https://www.ebi.ac.uk/pdbsum/2wv7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wv7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D0AB41_ALKCL D0AB41_ALKCL] 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wv/2wv7_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2wv7 ConSurf].
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== Publication Abstract from PubMed ==
The intracellular subtilisin proteases (ISPs) are the only known members of the important and ubiquitous subtilisin family that function exclusively within the cell, constituting a major component of the degradome in many Gram-positive bacteria. The first ISP structure reported herein at a spacing of 1.56 A reveals features unique among subtilisins that has enabled potential functional and physiological roles to be assigned to sequence elements exclusive to the ISPs. Unlike all other subtilisins, ISP from B. clausii is dimeric, with residues from the C terminus making a major contribution to the dimer interface by crossing over to contact the partner subunit. A short N-terminal extension binds back across the active site to provide a potential novel regulatory mechanism of intrinsic proteolytic activity: a proline residue conserved throughout the ISPs introduces a kink in the polypeptide backbone that lifts the target peptide bond out of reach of the catalytic residues.

Crystal structure of an intracellular subtilisin reveals novel structural features unique to this subtilisin family.,Vevodova J, Gamble M, Kunze G, Ariza A, Dodson E, Jones DD, Wilson KS Structure. 2010 Jun 9;18(6):744-55. PMID:20541512<ref>PMID:20541512</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2wv7" style="background-color:#fffaf0;"></div>

==See Also==
*[[Subtilisin 3D structures|Subtilisin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Alkalihalobacillus clausii]]
[[Category: Large Structures]]
[[Category: Ariza A]]
[[Category: Dodson E]]
[[Category: Gamble M]]
[[Category: Jones DD]]
[[Category: Vevodova J]]
[[Category: Wilson KS]]