View source for 2vhs


==Cathsilicatein, a chimera==
<StructureSection load='2vhs' size='340' side='right'caption='[[2vhs]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2vhs]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VHS 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]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2vhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vhs OCA], [https://pdbe.org/2vhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vhs RCSB], [https://www.ebi.ac.uk/pdbsum/2vhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vhs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CATL1_HUMAN CATL1_HUMAN] Important for the overall degradation of proteins in lysosomes.
== 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/vh/2vhs_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=2vhs ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cathepsin L mutants with the ability to condense silica from solution have been generated and a 1.5 A crystal structure of one of these chimeras allows us to rationalise the catalytic mechanism of silicic acid condensation.

Crystal structure and silica condensing activities of silicatein alpha-cathepsin L chimeras.,Fairhead M, Johnson KA, Kowatz T, McMahon SA, Carter LG, Oke M, Liu H, Naismith JH, van der Walle CF Chem Commun (Camb). 2008 Apr 21;(15):1765-7. Epub 2008 Feb 11. PMID:18379686<ref>PMID:18379686</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2vhs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Carter LG]]
[[Category: Fairhead M]]
[[Category: Johnson KA]]
[[Category: Kowatz T]]
[[Category: Liu H]]
[[Category: McMahon SA]]
[[Category: Naismith JH]]
[[Category: Oke M]]
[[Category: Wal CFVD]]