1xrl | pdb_00001xrl

Crystal structure of active site F1-mutant Y205F complex with inhibitor PCK

spinqualitylabelsall models 1xrl, resolution 1.82Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1xrl is a 1 chain structure with sequence from "thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PHK Related: 1mtz, 1mu0, 1mt3, 1xqv, 1xqw, 1xqx, 1xqy, 1xrm, 1xrn, 1xro, 1xrp, 1xrq, 1xrr Gene: TA0830 ("Thermoplasma acidophila" (sic) Darland et al. 1970) Activity: Prolyl aminopeptidase, with EC number 3.4.11.5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PIP_THEAC] Cleaves H-Pro-AMC as well as a wide spectrum of amino acid substrates and several peptide substrates without a proline at the N-terminus. Proteases F1, F2 and F3 degrade oligopeptides produced by Tricorn (themselves probably produced by the proteasome) yielding free amino acids. 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 tricorn-interacting factor F1 of the archaeon Thermoplasma acidophilum cleaves small hydrophobic peptide products of the proteasome and tricorn protease. F1 mutants of the active site residues that are involved in substrate recognition and catalysis displayed distinct activity patterns toward fluorogenic test substrates. Crystal structures of the mutant proteins complexed with peptides Phe-Leu, Pro-Pro, or Pro-Leu-Gly-Gly showed interaction of glutamates 213 and 245 with the N termini of the peptides and defined the S1 and S1' sites and the role of the catalytic residues. Evidence was found for processive peptide cleavage in the N-to-C direction, whereby the P1' product is translocated into the S1 site. A functional interaction of F1 with the tricorn protease was observed with the inactive F1 mutant G37A. Moreover, small angle x-ray scattering measurements for tricorn and inhibited F1 have been interpreted as formation of transient and substrate-induced complexes. X-ray snapshots of peptide processing in mutants of tricorn-interacting factor F1 from Thermoplasma acidophilum.,Goettig P, Brandstetter H, Groll M, Gohring W, Konarev PV, Svergun DI, Huber R, Kim JS J Biol Chem. 2005 Sep 30;280(39):33387-96. Epub 2005 Jul 1. PMID:15994304 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aminopeptidase 3D structures

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