4X8I
de novo crystal structure of the Pyrococcus Furiosus TET3 aminopeptidase
Summary for 4X8I
| Entry DOI | 10.2210/pdb4x8i/pdb |
| Descriptor | Lysyl aminopeptidase, ZINC ION, COBALT (II) ION, ... (7 entities in total) |
| Functional Keywords | aminopeptidase, hydrolase |
| Biological source | Pyrococcus furiosus |
| Total number of polymer chains | 3 |
| Total formula weight | 117405.72 |
| Authors | Colombo, M. (deposition date: 2014-12-10, release date: 2016-02-10, Last modification date: 2024-05-08) |
| Primary citation | Colombo, M.,Girard, E.,Franzetti, B. Tuned by metals: the TET peptidase activity is controlled by 3 metal binding sites. Sci Rep, 6:20876-20876, 2016 Cited by PubMed Abstract: 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. PubMed: 26853450DOI: 10.1038/srep20876 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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