View source for 4qhg


==Crystal structure of Methanocaldococcus jannaschii dimeric selecase==
<StructureSection load='4qhg' size='340' side='right'caption='[[4qhg]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4qhg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii_DSM_2661 Methanocaldococcus jannaschii DSM 2661]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QHG 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4qhg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qhg OCA], [https://pdbe.org/4qhg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qhg RCSB], [https://www.ebi.ac.uk/pdbsum/4qhg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qhg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Y1213_METJA Y1213_METJA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Molecular plasticity controls enzymatic activity: the native fold of a protein in a given environment is normally unique and at a global free-energy minimum. Some proteins, however, spontaneously undergo substantial fold switching to reversibly transit between defined conformers, the "metamorphic" proteins. Here, we present a minimal metamorphic, selective, and specific caseinolytic metallopeptidase, selecase, which reversibly transits between several different states of defined three-dimensional structure, which are associated with loss of enzymatic activity due to autoinhibition. The latter is triggered by sequestering the competent conformation in incompetent but structured dimers, tetramers, and octamers. This system, which is compatible with a discrete multifunnel energy landscape, affords a switch that provides a reversible mechanism of control of catalytic activity unique in nature.

Multiple stable conformations account for reversible concentration-dependent oligomerization and autoinhibition of a metamorphic metallopeptidase.,Lopez-Pelegrin M, Cerda-Costa N, Cintas-Pedrola A, Herranz-Trillo F, Bernado P, Peinado JR, Arolas JL, Gomis-Ruth FX Angew Chem Int Ed Engl. 2014 Sep 26;53(40):10624-30. doi: 10.1002/anie.201405727., Epub 2014 Aug 27. PMID:25159620<ref>PMID:25159620</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4qhg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanocaldococcus jannaschii DSM 2661]]
[[Category: Arolas JL]]
[[Category: Bernado P]]
[[Category: Cerda-costa N]]
[[Category: Cintas-pedrola A]]
[[Category: Gomis-ruth FX]]
[[Category: Herranz-trillo F]]
[[Category: Lopez-pelegrin M]]
[[Category: Peinado JR]]