3sta: Difference between revisions

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 ==Crystal structure of ClpP in tetradecameric form from Staphylococcus aureus==
-<StructureSection load='3sta' size='340' side='right' caption='[[3sta]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
+<StructureSection load='3sta' size='340' side='right'caption='[[3sta]], [[Resolution|resolution]] 2.28&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3sta]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Staaw Staaw]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3STA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3STA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3sta]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_MW2 Staphylococcus aureus subsp. aureus MW2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3STA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3STA FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3st9|3st9]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.28&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=196620 STAAW])</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=3sta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sta OCA], [https://pdbe.org/3sta PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sta RCSB], [https://www.ebi.ac.uk/pdbsum/3sta PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sta ProSAT]</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=3sta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sta OCA], [http://pdbe.org/3sta PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3sta RCSB], [http://www.ebi.ac.uk/pdbsum/3sta PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3sta ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CLPP_STAAW CLPP_STAAW]] 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).
+[https://www.uniprot.org/uniprot/CLPP_STAAW CLPP_STAAW] 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;">
-== Publication Abstract from PubMed ==
-ATP-dependent Clp protease (ClpP) is an attractive new target for the development of anti-infective agents. The ClpP protease consists of two heptameric rings that enclose a large chamber containing 14 proteolytic active sites. Recent studies indicate that ClpP likely undergoes conformational switching between an extended and degraded active state required for substrate proteolysis and a compacted and catalytically inactive state allowing product release. Here, we present the wild-type ClpP structures in two distinct states from Staphylococcus aureus. One structure is very similar to those solved ClpP structures in the extended states. The other is strikingly different from both the extended and the compacted state as observed in ClpP from other species; the handle domain of this structure kinks to take on a compressed conformation. Structural analysis and molecular dynamic simulations show that the handle domain predominantly controls the way in which degradation products exit the chamber through dynamic conformational switching from the extended state to the compressed state. Given the highly conserved sequences among ClpP from different species, this compressed conformation is unexpected and novel, which is potentially valuable for understanding the enzymatic dynamics and the acting mechanisms of ClpP.
-Structural switching of Staphylococcus aureus Clp protease: a key to understanding protease dynamics.,Zhang J, Ye F, Lan L, Jiang H, Luo C, Yang CG J Biol Chem. 2011 Oct 28;286(43):37590-601. Epub 2011 Sep 7. PMID:21900233<ref>PMID:21900233</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3sta" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Clp Protease|Clp Protease]]
+*[[Clp protease 3D structures|Clp protease 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Endopeptidase Clp]]
+[[Category: Large Structures]]
-[[Category: Staaw]]
+[[Category: Staphylococcus aureus subsp. aureus MW2]]
-[[Category: Jiang, H]]
+[[Category: Jiang H]]
-[[Category: Lan, L]]
+[[Category: Lan L]]
-[[Category: Luo, C]]
+[[Category: Luo C]]
-[[Category: Yang, C G]]
+[[Category: Yang C-G]]
-[[Category: Ye, F]]
+[[Category: Ye F]]
-[[Category: Zhang, J]]
+[[Category: Zhang J]]
-[[Category: Atpase-dependent clp protease]]
-[[Category: Hydrolase]]