1mt3
From Proteopedia
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Crystal Structure of the Tricorn Interacting Factor Selenomethionine-F1
Overview
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.
About this Structure
1MT3 is a Single protein structure of sequence from Thermoplasma acidophilum with MES as ligand. Active as Prolyl aminopeptidase, with EC number 3.4.11.5 Full crystallographic information is available from OCA.
Reference
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
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