View source for 1kuh


==ZINC PROTEASE FROM STREPTOMYCES CAESPITOSUS==
<StructureSection load='1kuh' size='340' side='right'caption='[[1kuh]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1kuh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_caespitosus Streptomyces caespitosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KUH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KUH 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]] 1.6&#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=ZN:ZINC+ION'>ZN</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=1kuh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kuh OCA], [https://pdbe.org/1kuh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kuh RCSB], [https://www.ebi.ac.uk/pdbsum/1kuh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kuh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SNPA_STRCS SNPA_STRCS] Specifically hydrolyzes the peptide bond at the imino side of aromatic residues.
== 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/ku/1kuh_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1kuh ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A zinc endoprotease produced by Streptomyces caespitosus (ScNP) specifically hydrolyzes the peptide bond at the imino side of aromatic residues and is the smallest protease found to date. Although ScNP carries the zinc-binding sequence HEXXH, its primary structure of 132 amino acid residues differs from those of other known zinc metalloendoproteases. X-ray structural analysis of ScNP at 1.6 A resolution revealed that despite a lack of sequence homology, the common topological feature of main-chain folding and a beta-turn containing methionine, which is a feature of the zinc metalloendoprotease superfamily of metzincins, is conserved in ScNP. The zinc atom of ScNP is tetrahedrally ligated by the two histidines in the HEXXH sequence, an aspartate residue and a water molecule. Thus, ScNP represents a novel subfamily of metzincins with a HEXXHXXGXXD zinc-binding sequence. A plausible substrate recognition pocket to which aromatic residues bind is located near the catalytic zinc ion.

Structure of the zinc endoprotease from Streptomyces caespitosus.,Kurisu G, Kinoshita T, Sugimoto A, Nagara A, Kai Y, Kasai N, Harada S J Biochem. 1997 Feb;121(2):304-8. PMID:9089404<ref>PMID:9089404</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 1kuh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces caespitosus]]
[[Category: Harada S]]
[[Category: Kai Y]]
[[Category: Kasai N]]
[[Category: Kinoshita T]]
[[Category: Kurisu G]]
[[Category: Nagara A]]
[[Category: Sugimoto A]]