6f3k

Combined solid-state NMR, solution-state NMR and EM data for structure determination of the tetrahedral aminopeptidase TET2 from P. horikoshiiCombined solid-state NMR, solution-state NMR and EM data for structure determination of the tetrahedral aminopeptidase TET2 from P. horikoshii

Structural highlights

6f3k is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TET_PYRHO] Functions as an aminopeptidase, with a clear preference for leucine as the N-terminal amino acid. However, can also cleave moderately long polypeptide substrates of various compositions in a fairly unspecific manner. Has neither carboxypeptidase nor endoproteolytic activities, and it is devoid of N-terminal deblocking activity. Is involved in protein degradation, performing degradation of oligopeptides produced by the proteasome into single amino acids.^[1] ^[2] ^[3]

References

↑ Russo S, Baumann U. Crystal structure of a dodecameric tetrahedral-shaped aminopeptidase. J Biol Chem. 2004 Dec 3;279(49):51275-81. Epub 2004 Sep 16. PMID:15375159 doi:10.1074/jbc.M409455200
↑ Borissenko L, Groll M. Crystal structure of TET protease reveals complementary protein degradation pathways in prokaryotes. J Mol Biol. 2005 Mar 11;346(5):1207-19. Epub 2005 Jan 16. PMID:15713475 doi:10.1016/j.jmb.2004.12.056
↑ Dura MA, Receveur-Brechot V, Andrieu JP, Ebel C, Schoehn G, Roussel A, Franzetti B. Characterization of a TET-like aminopeptidase complex from the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemistry. 2005 Mar 8;44(9):3477-86. PMID:15736957 doi:http://dx.doi.org/10.1021/bi047736j

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OCA

[1] Russo S, Baumann U. Crystal structure of a dodecameric tetrahedral-shaped aminopeptidase. J Biol Chem. 2004 Dec 3;279(49):51275-81. Epub 2004 Sep 16. PMID:15375159 doi:10.1074/jbc.M409455200

[2] Borissenko L, Groll M. Crystal structure of TET protease reveals complementary protein degradation pathways in prokaryotes. J Mol Biol. 2005 Mar 11;346(5):1207-19. Epub 2005 Jan 16. PMID:15713475 doi:10.1016/j.jmb.2004.12.056

[3] Dura MA, Receveur-Brechot V, Andrieu JP, Ebel C, Schoehn G, Roussel A, Franzetti B. Characterization of a TET-like aminopeptidase complex from the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemistry. 2005 Mar 8;44(9):3477-86. PMID:15736957 doi:http://dx.doi.org/10.1021/bi047736j

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