1y0r
From Proteopedia
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| - | [[Image:1y0r.gif|left|200px]] | + | [[Image:1y0r.gif|left|200px]] |
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| - | '''Crystal structure of the tetrahedral aminopeptidase from P. horikoshii''' | + | {{Structure |
| + | |PDB= 1y0r |SIZE=350|CAPTION= <scene name='initialview01'>1y0r</scene>, resolution 1.75Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=ARS:ARSENIC'>ARS</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the tetrahedral aminopeptidase from P. horikoshii''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1Y0R is a [ | + | 1Y0R is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y0R OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15713475 15713475] |
[[Category: Pyrococcus horikoshii]] | [[Category: Pyrococcus horikoshii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: pdz domain]] | [[Category: pdz domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:17:00 2008'' |
Revision as of 13:17, 20 March 2008
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| , resolution 1.75Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the tetrahedral aminopeptidase from P. horikoshii
Overview
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 Structure
1Y0R is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.
Reference
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
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