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==de novo crystal structure of the Pyrococcus Furiosus TET3 aminopeptidase== | ==de novo crystal structure of the Pyrococcus Furiosus TET3 aminopeptidase== | ||
<StructureSection load='4x8i' size='340' side='right' caption='[[4x8i]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='4x8i' size='340' side='right' caption='[[4x8i]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/AMPK_PYRFU 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. | [[http://www.uniprot.org/uniprot/AMPK_PYRFU 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. | ||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:26853450</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4x8i" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 22:35, 10 May 2016
de novo crystal structure of the Pyrococcus Furiosus TET3 aminopeptidasede novo crystal structure of the Pyrococcus Furiosus TET3 aminopeptidase
Structural highlights
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 PubMedTET 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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