5g1s

Open conformation of Francisella tularensis ClpP at 1.7 A

spinqualitylabelsall models 5g1s, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5g1s is a 21 chain structure with sequence from "bacterium_tularense"_mccoy_and_chapin_1912 "bacterium tularense" mccoy and chapin 1912. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, MPD, MRD Related: 5g1q, 5g1r Gene: clpP, DR86_1343 ("Bacterium tularense" McCoy and Chapin 1912) Activity: Endopeptidase Clp, with EC number 3.4.21.92 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [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] 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Clp Protease

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