1mt3 | pdb_00001mt3

Crystal Structure of the Tricorn Interacting Factor Selenomethionine-F1

spinqualitylabelsall models 1mt3, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1mt3 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: MES NonStd Res: MSE Related: 1mtz, 1mu0 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 F1 is a 33.5 kDa serine peptidase of the alpha/beta-hydrolase family from the archaeon Thermoplasma acidophilum. Subsequent to proteasomal protein degradation, tricorn generates small peptides, which are cleaved by F1 to yield single amino acids. We have solved the crystal structure of F1 with multiwavelength anomalous dispersion (MAD) phasing at 1.8 A resolution. In addition to the conserved catalytic domain, the structure reveals a chiefly alpha-helical domain capping the catalytic triad. Thus, the active site is accessible only through a narrow opening from the protein surface. Two structures with molecules bound to the active serine, including the inhibitor phenylalanyl chloromethylketone, elucidate the N-terminal recognition of substrates and the catalytic activation switch mechanism of F1. The cap domain mainly confers the specificity for hydrophobic side chains by a novel cavity system, which, analogously to the tricorn protease, guides substrates to the buried active site and products away from it. Finally, the structure of F1 suggests a possible functional complex with tricorn that allows efficient processive degradation to free amino acids for cellular recycling. Structures of the tricorn-interacting aminopeptidase F1 with different ligands explain its catalytic mechanism.,Goettig P, Groll M, Kim JS, Huber R, Brandstetter H EMBO J. 2002 Oct 15;21(20):5343-52. PMID:12374735 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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