3lxu
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3lxu is ON HOLD Authors: Chuang, C.K. Description: Crystal Structure of Tripeptidyl Peptidase 2 (TPP II) ''Page seeded by [http://oca.weizmann.ac....) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of Tripeptidyl Peptidase 2 (TPP II)== | |
| + | <StructureSection load='3lxu' size='340' side='right'caption='[[3lxu]], [[Resolution|resolution]] 3.14Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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='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='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='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> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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 == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <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/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lxu ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:20676100</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3lxu" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| + | *[[Tripeptidyl peptidase|Tripeptidyl peptidase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Drosophila melanogaster]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chuang CK]] | ||
Current revision
Crystal Structure of Tripeptidyl Peptidase 2 (TPP II)
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