View source for 4ryf


==ClpP1/2 heterocomplex from Listeria monocytogenes==
<StructureSection load='4ryf' size='340' side='right'caption='[[4ryf]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ryf]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RYF 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]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <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=4ryf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ryf OCA], [https://pdbe.org/4ryf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ryf RCSB], [https://www.ebi.ac.uk/pdbsum/4ryf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ryf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8Y7Y1_LISMO Q8Y7Y1_LISMO] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity).[HAMAP-Rule:MF_00444]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Listeria monocytogenes is a devastating bacterial pathogen. Its virulence and intracellular stress tolerance are supported by caseinolytic protease P (ClpP), an enzyme that is conserved among bacteria. L. monocytogenes expresses two ClpP isoforms that are only distantly related by sequence and differ in catalysis, oligomerization, active-site composition, and N-terminal interaction sites for associated AAA(+) chaperones. The crystal structure of the ClpP1/2 heterocomplex from L. monocytogenes was solved, and in combination with biochemical studies, it provides insights into the mode of action. The results demonstrate that structural interlocking of LmClpP1 with LmClpP2 leads to the formation of a tetradecamer, aligns all 14 active sites, and enhances proteolytic activity. Furthermore, the catalytic center was identified as being responsible for the transient stability of ClpPs.

Structure and mechanism of the caseinolytic protease ClpP1/2 heterocomplex from Listeria monocytogenes.,Dahmen M, Vielberg MT, Groll M, Sieber SA Angew Chem Int Ed Engl. 2015 Mar 16;54(12):3598-602. doi: 10.1002/anie.201409325., Epub 2015 Jan 28. PMID:25630955<ref>PMID:25630955</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ryf" style="background-color:#fffaf0;"></div>

==See Also==
*[[Clp protease 3D structures|Clp protease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Listeria monocytogenes]]
[[Category: Dahmen M]]
[[Category: Groll M]]
[[Category: Sieber SA]]
[[Category: Vielberg M-T]]