3v5i: Difference between revisions
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{{Large structure}} | |||
==The crystal structure of the mutant ClpP S98A (Staphylococcus aureus)== | ==The crystal structure of the mutant ClpP S98A (Staphylococcus aureus)== | ||
<StructureSection load='3v5i' size='340' side='right' caption='[[3v5i]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='3v5i' size='340' side='right' caption='[[3v5i]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3v5i]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3v5i]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/Staa8 Staa8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V5I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3V5I FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qwd|3qwd]], [[3v5e|3v5e]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qwd|3qwd]], [[3v5e|3v5e]]</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= | <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=93061 STAA8])</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=3v5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v5i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3v5i RCSB], [http://www.ebi.ac.uk/pdbsum/3v5i PDBsum]</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=3v5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v5i OCA], [http://pdbe.org/3v5i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3v5i RCSB], [http://www.ebi.ac.uk/pdbsum/3v5i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3v5i ProSAT]</span></td></tr> | ||
</table> | </table> | ||
{{Large structure}} | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/CLPP_STAA8 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). | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3v5i" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Clp Protease|Clp Protease]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Endopeptidase Clp]] | [[Category: Endopeptidase Clp]] | ||
[[Category: | [[Category: Staa8]] | ||
[[Category: Gersch, M]] | [[Category: Gersch, M]] | ||
[[Category: Groll, M]] | [[Category: Groll, M]] | ||
Revision as of 12:44, 11 August 2016
The crystal structure of the mutant ClpP S98A (Staphylococcus aureus)The crystal structure of the mutant ClpP S98A (Staphylococcus aureus)
Structural highlights
Warning: this is a large structure, and loading might take a long time or not happen at all. 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 PubMedThe barrel-shaped caseinolytic protease P (ClpP) is a main virulence regulator in the bacterial pathogen Staphylococcus aureus (SaClpP). It consists of two heptameric rings forming a homotetradecamer with an inner chamber that houses the 14 active sites. We recently showed that SaClpP is able to adopt a compressed, inactive conformation. We present here the 2.3 A resolution structure of SaClpP in its closed, active conformation as well as the structure of the S98A mutant. Comprehensive mutational analysis aiming at destabilizing one or the other or both conformations was able to pinpoint key residues involved in this catalytic switch and in the heptamer-heptamer interaction. By probing the active site serine with a covalently modifying beta-lactone probe, we could show that the tetradecameric organization is essential for a proper formation of the active site. Structural data suggest that a highly conserved hydrogen-bonding network links oligomerization to activity. A comparison of ClpP structures from different organisms provides suggestive evidence for the presence of a universal mechanism regulating ClpP activity in which binding of one subunit to the corresponding subunit on the other ring interface is necessary for the functional assembly of the catalytic triad and thus for protease function. This mechanism ensures controlled access to the active sites of a highly unspecific protease. Insights into structural network responsible for oligomerization and activity of bacterial virulence regulator caseinolytic protease P (ClpP) protein.,Gersch M, List A, Groll M, Sieber SA J Biol Chem. 2012 Mar 16;287(12):9484-94. Epub 2012 Jan 30. PMID:22291011[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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