2cea

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[[Image:2cea.png|left|200px]]
 
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==CELL DIVISION PROTEIN FTSH==
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The line below this paragraph, containing "STRUCTURE_2cea", creates the "Structure Box" on the page.
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<StructureSection load='2cea' size='340' side='right'caption='[[2cea]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2cea]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CEA FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
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<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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_2cea| PDB=2cea | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cea OCA], [https://pdbe.org/2cea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cea RCSB], [https://www.ebi.ac.uk/pdbsum/2cea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cea ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FTSH_THEMA FTSH_THEMA] 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.[HAMAP-Rule:MF_01458]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ce/2cea_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2cea ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The ATP-dependent integral membrane protease FtsH is universally conserved in bacteria. Orthologs exist in chloroplasts and mitochondria, where in humans the loss of a close FtsH-homolog causes a form of spastic paraplegia. FtsH plays a crucial role in quality control by degrading unneeded or damaged membrane proteins, but it also targets soluble signaling factors like sigma(32) and lambda-CII. We report here the crystal structure of a soluble FtsH construct that is functional in caseinolytic and ATPase assays. The molecular architecture of this hexameric molecule consists of two rings where the protease domains possess an all-helical fold and form a flat hexagon that is covered by a toroid built by the AAA domains. The active site of the protease classifies FtsH as an Asp-zincin, contrary to a previous report. The different symmetries of protease and AAA rings suggest a possible translocation mechanism of the target polypeptide chain into the interior of the molecule where the proteolytic sites are located.
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===CELL DIVISION PROTEIN FTSH===
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The molecular architecture of the metalloprotease FtsH.,Bieniossek C, Schalch T, Bumann M, Meister M, Meier R, Baumann U Proc Natl Acad Sci U S A. 2006 Feb 28;103(9):3066-71. Epub 2006 Feb 16. PMID:16484367<ref>PMID:16484367</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_16484367}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2cea" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16484367 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16484367}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[2cea]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CEA OCA].
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==Reference==
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<ref group="xtra">PMID:016484367</ref><references group="xtra"/>
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[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Baumann, U.]]
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[[Category: Baumann U]]
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[[Category: Bieniossek, C.]]
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[[Category: Bieniossek C]]
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[[Category: Cell division]]
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[[Category: Hydrolase]]
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[[Category: Metalloprotease]]
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Current revision

CELL DIVISION PROTEIN FTSH

PDB ID 2cea

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