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| | <StructureSection load='1y0y' size='340' side='right'caption='[[1y0y]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='1y0y' size='340' side='right'caption='[[1y0y]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1y0y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/'pyrococcus_shinkaii' 'pyrococcus shinkaii']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y0Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1y0y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] and [https://en.wikipedia.org/wiki/Streptomyces_sp._ME98-M3 Streptomyces sp. ME98-M3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y0Y FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=L2O:(2S,3R)-3-AMINO-2-HYDROXY-5-METHYLHEXANOIC+ACID'>L2O</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=L2O:(2S,3R)-3-AMINO-2-HYDROXY-5-METHYLHEXANOIC+ACID'>L2O</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1xfo|1xfo]], [[1vhe|1vhe]], [[1vho|1vho]], [[1y0r|1y0r]]</div></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1y0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y0y OCA], [https://pdbe.org/1y0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y0y RCSB], [https://www.ebi.ac.uk/pdbsum/1y0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y0y ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1y0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y0y OCA], [https://pdbe.org/1y0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y0y RCSB], [https://www.ebi.ac.uk/pdbsum/1y0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y0y ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TET_PYRHO 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.<ref>PMID:15375159</ref> <ref>PMID:15713475</ref> <ref>PMID:15736957</ref>
| + | [https://www.uniprot.org/uniprot/TET_PYRHO 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.<ref>PMID:15375159</ref> <ref>PMID:15713475</ref> <ref>PMID:15736957</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Pyrococcus shinkaii]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Borissenko, L]] | + | [[Category: Pyrococcus horikoshii]] |
| - | [[Category: Groll, M]] | + | [[Category: Streptomyces sp. ME98-M3]] |
| - | [[Category: Aminopeptidase]] | + | [[Category: Borissenko L]] |
| - | [[Category: Hydrolase-hydrolase inhibitor complex]] | + | [[Category: Groll M]] |
| - | [[Category: Pdz]]
| + | |
| Structural highlights
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]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
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
- ↑ 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
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