5c90: Difference between revisions
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==Staphylococcus aureus ClpP mutant - Y63A== | ==Staphylococcus aureus ClpP mutant - Y63A== | ||
<StructureSection load='5c90' size='340' side='right' caption='[[5c90]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='5c90' size='340' side='right'caption='[[5c90]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5c90]] is a 14 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C90 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C90 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5c90]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C90 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C90 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpP, SAOUHSC_00790 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_Clp Endopeptidase Clp], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.92 3.4.21.92] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_Clp Endopeptidase Clp], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.92 3.4.21.92] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5c90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c90 OCA], [http://pdbe.org/5c90 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c90 RCSB], [http://www.ebi.ac.uk/pdbsum/5c90 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c90 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5c90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c90 OCA], [http://pdbe.org/5c90 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c90 RCSB], [http://www.ebi.ac.uk/pdbsum/5c90 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c90 ProSAT]</span></td></tr> | ||
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</div> | </div> | ||
<div class="pdbe-citations 5c90" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5c90" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Clp protease 3D structures|Clp protease 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Endopeptidase Clp]] | [[Category: Endopeptidase Clp]] | ||
[[Category: Large Structures]] | |||
[[Category: Gan, J]] | [[Category: Gan, J]] | ||
[[Category: Liu, H]] | [[Category: Liu, H]] | ||
Revision as of 14:16, 18 March 2020
Staphylococcus aureus ClpP mutant - Y63AStaphylococcus aureus ClpP mutant - Y63A
Structural highlights
Function[CLPP_STAA8] 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). Publication Abstract from PubMedATP-dependent Clp protease (ClpP), a highly conserved serine protease in vast bacteria, could be converted into a noncontrollable enzyme capable of degrading mature proteins in the presence of acyldepsipeptides (ADEPs). Here, we design such a gain-of-function mutant of Staphylococcus aureus ClpP (SaClpP) capable of triggering the same level of dysfunctional activity that occurs upon ADEPs treatment. The SaClpPY63A mutant degrades FtsZ in vivo and inhibits staphylococcal growth. The crystal structure of SaClpPY63A indicates that Asn42 would be an important domino to fall for further activation of ClpP. Indeed, the SaClpPN42AY63A mutant demonstrates promoted self-activated proteolysis, which is a result of an enlarged entrance pore as observed in cryo-electron microscopy images. In addition, the expression of the engineered clpP allele phenocopies treatment with ADEPs; inhibition of cell division occurs as does showing sterilizing with rifampicin antibiotics. Collectively, we show that the gain-of-function SaClpPN42AY63A mutant becomes a fairly nonspecific protease and kills persisters by degrading over 500 proteins, thus providing new insights into the structure of the ClpP protease. Characterization of Gain-of-Function Mutant Provides New Insights into ClpP Structure.,Ni T, Ye F, Liu X, Zhang J, Liu H, Li J, Zhang Y, Sun Y, Wang M, Luo C, Jiang H, Lan L, Gan J, Zhang A, Zhou H, Yang CG ACS Chem Biol. 2016 May 17. PMID:27171654[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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