4x8i | pdb_00004x8i

de novo crystal structure of the Pyrococcus Furiosus TET3 aminopeptidase

spinqualitylabelsall models 4x8i, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4x8i is a 3 chain structure with sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: CL, CO, DO3, GD, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AMPK_PYRFU Hydrolyzes di-, tri- and tetrapeptides with a lysine as the N-terminal amino acid and with Gly, Lys, Ala, Phe or Glu in the second position. Publication Abstract from PubMed TET aminopeptidases are dodecameric particles shared in the three life domains involved in various biological processes, from carbon source provider in archaea to eye-pressure regulation in humans. Each subunit contains a dinuclear metal site (M1 and M2) responsible for the enzyme catalytic activity. However, the role of each metal ion is still uncharacterized. Noteworthy, while mesophilic TETs are activated by Mn(2+), hyperthermophilic TETs prefers Co(2+). Here, by means of anomalous x-ray crystallography and enzyme kinetics measurements of the TET3 aminopeptidase from the hyperthermophilic organism Pyrococcus furiosus (PfTET3), we show that M2 hosts the catalytic activity of the enzyme, while M1 stabilizes the TET3 quaternary structure and controls the active site flexibility in a temperature dependent manner. A new third metal site (M3) was found in the substrate binding pocket, modulating the PfTET3 substrate preferences. These data show that TET activity is tuned by the molecular interplay among three metal sites. Tuned by metals: the TET peptidase activity is controlled by 3 metal binding sites.,Colombo M, Girard E, Franzetti B Sci Rep. 2016 Feb 8;6:20876. doi: 10.1038/srep20876. PMID:26853450 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aminopeptidase 3D structures

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