3st9

Crystal structure of ClpP in heptameric form from Staphylococcus aureus

spinqualitylabelsall models 3st9, resolution 2.43Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3st9 is a 7 chain structure with sequence from Staaw. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, GOL, SO4 Related: 3sta Gene: clpP (STAAW) Activity: Endopeptidase Clp, with EC number 3.4.21.92 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [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). 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Clp protease 3D structures

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