5g1r
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5g1r is ON HOLD Authors: Diaz-Saez, L., Hunter, W.N. Description: Open conformation of Francisella tularensis ClpP at 1.9 A [[Category: Unreleased ...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Open conformation of Francisella tularensis ClpP at 1.9 A== | |
| + | <StructureSection load='5g1r' size='340' side='right'caption='[[5g1r]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5g1r]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Francisella_tularensis Francisella tularensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G1R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G1R 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]] 1.9Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</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=5g1r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g1r OCA], [https://pdbe.org/5g1r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g1r RCSB], [https://www.ebi.ac.uk/pdbsum/5g1r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g1r ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CLPP_FRATT CLPP_FRATT] 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.[HAMAP-Rule:MF_00444] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Caseinolytic proteases are large oligomeric assemblies responsible for maintaining protein homeostasis in bacteria and in so doing influence a wide range of biological processes. The functional assembly involves three chaperones together with the oligomeric caseinolytic protease catalytic subunit P (ClpP). This protease represents a potential target for therapeutic intervention in pathogenic bacteria. Here, we detail an efficient protocol for production of recombinant ClpP from Francisella tularensis, and the structural characterization of three crystal forms which grow under similar conditions. One crystal form reveals a compressed state of the ClpP tetradecamer and two forms an open state. A comparison of the two types of structure infers that differences at the enzyme active site result from a conformational change involving a highly localized disorder-order transition of a beta-strand alpha-helix combination. This transition occurs at a subunit-subunit interface. Our study may now underpin future efforts in a structure-based approach to target ClpP for inhibitor or activator development. Proteins 2016; 85:188-194. (c) 2016 Wiley Periodicals, Inc. | ||
| - | + | Open and compressed conformations of Francisella tularensis ClpP.,Diaz-Saez L, Pankov G, Hunter WN Proteins. 2017 Jan;85(1):188-194. doi: 10.1002/prot.25197. Epub 2016 Nov 20. PMID:27802578<ref>PMID:27802578</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5g1r" style="background-color:#fffaf0;"></div> |
| - | [[Category: Diaz-Saez | + | |
| + | ==See Also== | ||
| + | *[[Clp protease 3D structures|Clp protease 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Francisella tularensis]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Diaz-Saez L]] | ||
| + | [[Category: Hunter WN]] | ||
Current revision
Open conformation of Francisella tularensis ClpP at 1.9 A
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