2dhr
From Proteopedia
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- | [[Image:2dhr.png|left|200px]] | ||
- | + | ==Whole cytosolic region of ATP-dependent metalloprotease FtsH (G399L)== | |
+ | <StructureSection load='2dhr' size='340' side='right'caption='[[2dhr]], [[Resolution|resolution]] 3.90Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2dhr]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DHR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DHR 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]] 3.9Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</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=2dhr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dhr OCA], [https://pdbe.org/2dhr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dhr RCSB], [https://www.ebi.ac.uk/pdbsum/2dhr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dhr ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/FTSH_THET8 FTSH_THET8] Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins (By similarity).[HAMAP-Rule:MF_01458] Degrades preferentially unfolded substrates in a processive, ATP-dependent manner, usually after hydrophobic residues.[HAMAP-Rule:MF_01458] | ||
+ | == 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/dh/2dhr_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2dhr ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | An ATP-dependent protease, FtsH, digests misassembled membrane proteins in order to maintain membrane integrity and digests short-lived soluble proteins in order to control their cellular regulation. This enzyme has an N-terminal transmembrane segment and a C-terminal cytosolic region consisting of an AAA+ ATPase domain and a protease domain. Here we present two crystal structures: the protease domain and the whole cytosolic region. The cytosolic region fully retains an ATP-dependent protease activity and adopts a three-fold-symmetric hexameric structure. The protease domains displayed a six-fold symmetry, while the AAA+ domains, each containing ADP, alternate two orientations relative to the protease domain, making "open" and "closed" interdomain contacts. Apparently, ATPase is active only in the closed form, and protease operates in the open form. The protease catalytic sites are accessible only through a tunnel following from the AAA+ domain of the adjacent subunit, raising a possibility of translocation of polypeptide substrate to the protease sites through this tunnel. | ||
- | + | Structure of the whole cytosolic region of ATP-dependent protease FtsH.,Suno R, Niwa H, Tsuchiya D, Zhang X, Yoshida M, Morikawa K Mol Cell. 2006 Jun 9;22(5):575-85. PMID:16762831<ref>PMID:16762831</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 2dhr" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | < | + | </StructureSection> |
+ | [[Category: Large Structures]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
- | [[Category: Morikawa | + | [[Category: Morikawa K]] |
- | [[Category: Niwa | + | [[Category: Niwa H]] |
- | [[Category: Suno | + | [[Category: Suno R]] |
- | [[Category: Tsuchiya | + | [[Category: Tsuchiya D]] |
- | [[Category: Yoshida | + | [[Category: Yoshida M]] |
- | [[Category: Zhang | + | [[Category: Zhang X]] |
- | + | ||
- | + | ||
- | + |
Current revision
Whole cytosolic region of ATP-dependent metalloprotease FtsH (G399L)
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