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3kds
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:3kds.jpg|left|200px]] | ||
| - | < | + | ==apo-FtsH crystal structure== |
| - | + | <StructureSection load='3kds' size='340' side='right'caption='[[3kds]], [[Resolution|resolution]] 2.60Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[3kds]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KDS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KDS FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NHX:N-{(2R)-2-[2-(HYDROXYAMINO)-2-OXOETHYL]-4-METHYLPENTANOYL}-3-NAPHTHALEN-2-YL-L-ALANYL-L-ALANINAMIDE'>NHX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | -- | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ce7|2ce7]], [[2cea|2cea]]</div></td></tr> |
| - | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FtsH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</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=3kds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kds OCA], [https://pdbe.org/3kds PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kds RCSB], [https://www.ebi.ac.uk/pdbsum/3kds PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kds 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/kd/3kds_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=3kds ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The hexameric membrane-spanning ATP-dependent metalloprotease FtsH is universally conserved in eubacteria, mitochondria, and chloroplasts, where it fulfills key functions in quality control and signaling. As a member of the self-compartmentalizing ATPases associated with various cellular activities (AAA+ proteases), FtsH converts the chemical energy stored in ATP via conformational rearrangements into a mechanical force that is used for substrate unfolding and translocation into the proteolytic chamber. The crystal structure of the ADP state of Thermotoga maritima FtsH showed a hexameric assembly consisting of a 6-fold symmetric protease disk and a 2-fold symmetric AAA ring. The 2.6 A resolution structure of the cytosolic region of apo-FtsH presented here reveals a new arrangement where the ATPase ring shows perfect 6-fold symmetry with the crucial pore residues lining an open circular entrance. Triggered by this conformational change, a substrate-binding edge beta strand appears within the proteolytic domain. Comparison of the apo- and ADP-bound structure visualizes an inward movement of the aromatic pore residues and generates a model of substrate translocation by AAA+ proteases. Furthermore, we demonstrate that mutation of a conserved glycine in the linker region inactivates FtsH. | ||
| - | + | The crystal structure of apo-FtsH reveals domain movements necessary for substrate unfolding and translocation.,Bieniossek C, Niederhauser B, Baumann UM Proc Natl Acad Sci U S A. 2009 Dec 22;106(51):21579-84. Epub 2009 Dec 2. PMID:19955424<ref>PMID:19955424</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | == | + | </div> |
| - | + | <div class="pdbe-citations 3kds" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| - | [[Category: Baumann, U | + | <references/> |
| - | [[Category: Bieniossek, C | + | __TOC__ |
| - | [[Category: Niederhauser, B | + | </StructureSection> |
| + | [[Category: Atcc 43589]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Baumann, U]] | ||
| + | [[Category: Bieniossek, C]] | ||
| + | [[Category: Niederhauser, B]] | ||
[[Category: Beta roll]] | [[Category: Beta roll]] | ||
[[Category: Met-turn]] | [[Category: Met-turn]] | ||
| - | + | [[Category: Metal binding protein]] | |
| - | + | ||
Current revision
apo-FtsH crystal structure
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