4jcr: Difference between revisions
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==ClpP1 N165D mutant from Listeria monocytogenes== | ==ClpP1 N165D mutant from Listeria monocytogenes== | ||
<StructureSection load='4jcr' size='340' side='right' caption='[[4jcr]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='4jcr' size='340' side='right'caption='[[4jcr]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4jcr]] is a 14 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4jcr]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes_EGD-e Listeria monocytogenes EGD-e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JCR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JCR FirstGlance]. <br> | ||
</td></tr> | </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=4jcr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jcr OCA], [https://pdbe.org/4jcr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jcr RCSB], [https://www.ebi.ac.uk/pdbsum/4jcr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jcr ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 19: | ||
==See Also== | ==See Also== | ||
*[[Clp | *[[Clp protease 3D structures|Clp protease 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Listeria monocytogenes EGD-e]] | ||
[[Category: Alte | [[Category: Alte F]] | ||
[[Category: Gersch | [[Category: Gersch M]] | ||
[[Category: Groll | [[Category: Groll M]] | ||
[[Category: List | [[Category: List A]] | ||
[[Category: Sieber | [[Category: Sieber S]] | ||
[[Category: Wachtel | [[Category: Wachtel R]] | ||
[[Category: Zeiler | [[Category: Zeiler E]] | ||
Revision as of 14:05, 24 November 2022
ClpP1 N165D mutant from Listeria monocytogenesClpP1 N165D mutant from Listeria monocytogenes
Structural highlights
FunctionQ8Y7Y1_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] Publication Abstract from PubMedCaseinolytic proteases (ClpPs) are large oligomeric protein complexes that contribute to cell homeostasis as well as virulence regulation in bacteria. Although most organisms possess a single ClpP protein, some organisms encode two or more ClpP isoforms. Here, we elucidated the crystal structures of ClpP1 and ClpP2 from pathogenic Listeria monocytogenes and observe an unprecedented regulation principle by the catalytic triad. Whereas L. monocytogenes (Lm)ClpP2 is both structurally and functionally similar to previously studied tetradecameric ClpP proteins from Escherichia coli and Staphylococcus aureus, heptameric LmClpP1 features an asparagine in its catalytic triad. Mutation of this asparagine to aspartate increased the reactivity of the active site and led to the assembly of a tetradecameric complex. We analyzed the heterooligomeric complex of LmClpP1 and LmClpP2 via coexpression and subsequent labeling studies with natural product-derived probes. Notably, the LmClpP1 peptidase activity is stimulated 75-fold in the complex providing insights into heterooligomerization as a regulatory mechanism. Collectively, our data point toward different preferences for substrates and inhibitors of the two ClpP enzymes and highlight their structural and functional characteristics. Structural and functional insights into caseinolytic proteases reveal an unprecedented regulation principle of their catalytic triad.,Zeiler E, List A, Alte F, Gersch M, Wachtel R, Poreba M, Drag M, Groll M, Sieber SA Proc Natl Acad Sci U S A. 2013 Jul 9;110(28):11302-7. doi:, 10.1073/pnas.1219125110. Epub 2013 Jun 24. PMID:23798410[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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