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| | ==Open conformation of Francisella tularensis ClpP at 1.7 A== | | ==Open conformation of Francisella tularensis ClpP at 1.7 A== |
| - | <StructureSection load='5g1s' size='340' side='right' caption='[[5g1s]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='5g1s' size='340' side='right'caption='[[5g1s]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5g1s]] is a 21 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_tularense"_mccoy_and_chapin_1912 "bacterium tularense" mccoy and chapin 1912]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G1S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5G1S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5g1s]] is a 21 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=5G1S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G1S FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5g1q|5g1q]], [[5g1r|5g1r]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clpP, DR86_1343 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=263 "Bacterium tularense" McCoy and Chapin 1912])</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=5g1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g1s OCA], [https://pdbe.org/5g1s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g1s RCSB], [https://www.ebi.ac.uk/pdbsum/5g1s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g1s 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=5g1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g1s OCA], [http://pdbe.org/5g1s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g1s RCSB], [http://www.ebi.ac.uk/pdbsum/5g1s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g1s ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A0E2ZNT9_FRATU A0A0E2ZNT9_FRATU]] 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][RuleBase:RU000550][SAAS:SAAS00674840] | + | [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;">
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| - | == Publication Abstract from PubMed ==
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| - | 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.
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| - | 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>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 5g1s" style="background-color:#fffaf0;"></div>
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Clp Protease|Clp Protease]] | + | *[[Clp protease 3D structures|Clp protease 3D structures]] |
| - | == References ==
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| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacterium tularense mccoy and chapin 1912]] | + | [[Category: Francisella tularensis]] |
| - | [[Category: Endopeptidase Clp]] | + | [[Category: Large Structures]] |
| - | [[Category: Diaz-Saez, L]] | + | [[Category: Diaz-Saez L]] |
| - | [[Category: Hunter, W N]] | + | [[Category: Hunter WN]] |
| - | [[Category: Pankov, G]] | + | [[Category: Pankov G]] |
| - | [[Category: Hydrolase]]
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