1Y0R

Crystal structure of the tetrahedral aminopeptidase from P. horikoshii

Summary for 1Y0R

• Entry DOI: 10.2210/pdb1y0r/pdb
• Related: 1VHE 1XFO 1Y0Y
• Descriptor: Frv operon protein FrvX, ZINC ION, ARSENIC, ... (4 entities in total)
• Functional Keywords: aminopeptidase domain, pdz domain, hydrolase
• Biological source: Pyrococcus horikoshii
• Total number of polymer chains: 1
• Total formula weight: 39276.77

Authors

Groll, M.,Borissenko, L. (deposition date: 2004-11-16, release date: 2005-03-01, Last modification date: 2024-03-13)

Primary citation

Borissenko, L.,Groll, M.
Crystal Structure of TET Protease Reveals Complementary Protein Degradation Pathways in Prokaryotes
J.Mol.Biol., 346:1207-1219, 2005

PubMed Abstract: Protein degradation is an essential and strictly controlled process with proteasome and functionally related proteases representing its central part. Tricorn protease (TRI) has been shown to act downstream of the proteasome, degrading produced peptides. Recently, a novel large prokaryotic aminopeptidase oligomeric complex, named TET, has been identified. This complex degrades peptides of different length in organisms where TRI is not present. We determined the crystal structure of TET from the thermophilic archaeon Pyrococcus horikoshii at 1.6 A resolution in native form and in complex with the inhibitor amastatin. We demonstrate that, beside the novel tetrahedral oligomerisation pattern, TET possesses a unique mechanism of substrate attraction and orientation. TET sequentially degrades peptides produced by the proteasome to single amino acids. Furthermore, we reconstituted in vitro the minimal protein degradation system from initial unfolding of labelled protein substrates, up to release of free amino acids. We propose that TET and TRI act as functional analogues in different organisms, with TET being more widely distributed. Thus, TET and TRI represent two evolutionarily diverged pathways of peptide degradation in prokaryotes.

PubMed: 15713475
DOI: 10.1016/j.jmb.2004.12.056

Experimental method

X-RAY DIFFRACTION (1.75 Å)