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| | ==Crystal Structure of Tripeptidyl Peptidase 2 (TPP II)== | | ==Crystal Structure of Tripeptidyl Peptidase 2 (TPP II)== |
| - | <StructureSection load='3lxu' size='340' side='right' caption='[[3lxu]], [[Resolution|resolution]] 3.14Å' scene=''> | + | <StructureSection load='3lxu' size='340' side='right'caption='[[3lxu]], [[Resolution|resolution]] 3.14Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3lxu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LXU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LXU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3lxu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LXU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LXU FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 3.14Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CG3991, TPP II, TppII ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tripeptidyl-peptidase_II Tripeptidyl-peptidase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.10 3.4.14.10] </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=3lxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lxu OCA], [https://pdbe.org/3lxu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lxu RCSB], [https://www.ebi.ac.uk/pdbsum/3lxu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lxu ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3lxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lxu OCA], [http://pdbe.org/3lxu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lxu RCSB], [http://www.ebi.ac.uk/pdbsum/3lxu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lxu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TPP2_DROME TPP2_DROME]] Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited (By similarity). Efficiently cleaves Ala-Ala-Ala-polypeptide and Pro-Pro-Ala-polypeptide, Val-Leu-Lys-polypeptide only at high concentration. Does not cleave Ala-Phe-Pro-polypeptide nor Pro-Leu-Gly-polypeptide. | + | [https://www.uniprot.org/uniprot/TPP2_DROME TPP2_DROME] Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited (By similarity). Efficiently cleaves Ala-Ala-Ala-polypeptide and Pro-Pro-Ala-polypeptide, Val-Leu-Lys-polypeptide only at high concentration. Does not cleave Ala-Phe-Pro-polypeptide nor Pro-Leu-Gly-polypeptide. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lx/3lxu_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lx/3lxu_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| - | [[Category: Tripeptidyl-peptidase II]] | + | [[Category: Large Structures]] |
| - | [[Category: Chuang, C K]] | + | [[Category: Chuang CK]] |
| - | [[Category: Aminopeptidase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Serine protease]]
| + | |
| - | [[Category: Spindle complex]]
| + | |
| Structural highlights
Function
TPP2_DROME Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited (By similarity). Efficiently cleaves Ala-Ala-Ala-polypeptide and Pro-Pro-Ala-polypeptide, Val-Leu-Lys-polypeptide only at high concentration. Does not cleave Ala-Phe-Pro-polypeptide nor Pro-Leu-Gly-polypeptide.
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
Tripeptidyl peptidase II (TPP II) is the largest known eukaryotic protease (6 MDa). It is believed to act downstream of the 26S proteasome, cleaving tripeptides from the N termini of longer peptides, and it is implicated in numerous cellular processes. Here we report the structure of Drosophila TPP II determined by a hybrid approach. We solved the structure of the dimer by X-ray crystallography and docked it into the three-dimensional map of the holocomplex, which we obtained by single-particle cryo-electron microscopy. The resulting structure reveals the compartmentalization of the active sites inside a system of chambers and suggests the existence of a molecular ruler determining the size of the cleavage products. Furthermore, the structure suggests a model for activation of TPP II involving the relocation of a flexible loop and a repositioning of the active-site serine, coupling it to holocomplex assembly and active-site sequestration.
Hybrid molecular structure of the giant protease tripeptidyl peptidase II.,Chuang CK, Rockel B, Seyit G, Walian PJ, Schonegge AM, Peters J, Zwart PH, Baumeister W, Jap BK Nat Struct Mol Biol. 2010 Aug;17(8):990-6. Epub 2010 Aug 1. PMID:20676100[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chuang CK, Rockel B, Seyit G, Walian PJ, Schonegge AM, Peters J, Zwart PH, Baumeister W, Jap BK. Hybrid molecular structure of the giant protease tripeptidyl peptidase II. Nat Struct Mol Biol. 2010 Aug;17(8):990-6. Epub 2010 Aug 1. PMID:20676100 doi:10.1038/nsmb.1870
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