2ce7: Difference between revisions

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-{{Seed}}
-[[Image:2ce7.png|left|200px]]
-<!--
+==EDTA treated==
-The line below this paragraph, containing "STRUCTURE_2ce7", creates the "Structure Box" on the page.
+<StructureSection load='2ce7' size='340' side='right'caption='[[2ce7]], [[Resolution|resolution]] 2.44&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2ce7]] 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=2CE7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CE7 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.44&#8491;</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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-{{STRUCTURE_2ce7|  PDB=2ce7  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ce7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ce7 OCA], [https://pdbe.org/2ce7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ce7 RCSB], [https://www.ebi.ac.uk/pdbsum/2ce7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ce7 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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]
+== 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/ce/2ce7_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=2ce7 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-===EDTA TREATED===
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_16484367}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2ce7" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 16484367 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16484367}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-CE7 is a [[Single protein]] structure of 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=2CE7 OCA].
-==Reference==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/16484367 16484367]
-[[Category: Single protein]]
 [[Category: Thermotoga maritima]]
-[[Category: Baumann, U.]]
+[[Category: Baumann U]]
-[[Category: Bieniossek, C.]]
+[[Category: Bieniossek C]]
-[[Category: Cell division]]
-[[Category: Cell division protein]]
-[[Category: Ftsh]]
-[[Category: Metalloprotease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:44:42 2008''