1y0r: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1y0r |SIZE=350|CAPTION= <scene name='initialview01'>1y0r</scene>, resolution 1.75Å | |PDB= 1y0r |SIZE=350|CAPTION= <scene name='initialview01'>1y0r</scene>, resolution 1.75Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ARS:ARSENIC'>ARS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1xfo|1XFO]], [[1vhe|1VHE]], [[1y0y|1Y0Y]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y0r OCA], [http://www.ebi.ac.uk/pdbsum/1y0r PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1y0r RCSB]</span> | |||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Borissenko, L.]] | [[Category: Borissenko, L.]] | ||
[[Category: Groll, M.]] | [[Category: Groll, M.]] | ||
[[Category: aminopeptidase domain]] | [[Category: aminopeptidase domain]] | ||
[[Category: pdz domain]] | [[Category: pdz domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:57:15 2008'' | ||
Revision as of 00:57, 31 March 2008
| |||||||
| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1XFO, 1VHE, 1Y0Y
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the tetrahedral aminopeptidase from P. horikoshii
OverviewOverview
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.
About this StructureAbout this Structure
1Y0R is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of TET protease reveals complementary protein degradation pathways in prokaryotes., Borissenko L, Groll M, J Mol Biol. 2005 Mar 11;346(5):1207-19. Epub 2005 Jan 16. PMID:15713475
Page seeded by OCA on Mon Mar 31 00:57:15 2008