3hln

Crystal structure of ClpP A153C mutant with inter-heptamer disulfide bonds

spinqualitylabelsall models 3hln, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3hln is a 28 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA Gene: b0437, clpP, JW0427, lopP (Escherichia coli) Activity: Endopeptidase Clp, with EC number 3.4.21.92 Resources: FirstGlance, OCA, RCSB, PDBsum Function [CLPP_ECOLI] 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. May play the role of a master protease which is attracted to different substrates by different specificity factors such as ClpA or ClpX. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The highly conserved ClpP protease consists of two heptameric rings that interact by the interdigitation of an alpha-helix beta strand handle domain motif to form a tetradecameric cylinder. We previously proposed that protease dynamics results in the temporary unstructuring of interacting pairs of handle domains, opening transient equatorial side pores that allow for peptide egress. Here, we report the structure of an Escherichia coli ClpP mutant in which each opposing pair of protomers is linked by a disulfide bond. This structure resembles the compact structures of Streptococcus pneumoniae, Mycobacterium tuberculosis, and Plasmodium falciparum ClpPs, rather than the active, extended structures that have previously been determined for E. coli ClpPs. The structural data, along with normal mode analysis, support a model whereby the ClpP cylinder switches dynamically between an active extended state required for substrate degradation and an inactive compact state allowing peptide product release. Structural and theoretical studies indicate that the cylindrical protease ClpP samples extended and compact conformations.,Kimber MS, Yu AY, Borg M, Leung E, Chan HS, Houry WA Structure. 2010 Jul 14;18(7):798-808. PMID:20637416 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Jmol/Visualizing large molecules

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