1iy1: Difference between revisions
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==Crystal structure of the FtsH ATPase domain with ADP from Thermus thermophilus== | ==Crystal structure of the FtsH ATPase domain with ADP from Thermus thermophilus== | ||
<StructureSection load='1iy1' size='340' side='right' caption='[[1iy1]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='1iy1' size='340' side='right' caption='[[1iy1]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ixz|1ixz]], [[1iy0|1iy0]], [[1iy2|1iy2]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ixz|1ixz]], [[1iy0|1iy0]], [[1iy2|1iy2]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FtsH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FtsH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iy1 OCA], [http://pdbe.org/1iy1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iy1 RCSB], [http://www.ebi.ac.uk/pdbsum/1iy1 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iy1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iy1 OCA], [http://pdbe.org/1iy1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iy1 RCSB], [http://www.ebi.ac.uk/pdbsum/1iy1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1iy1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iy/1iy1_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iy/1iy1_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 12:20, 17 January 2018
Crystal structure of the FtsH ATPase domain with ADP from Thermus thermophilusCrystal structure of the FtsH ATPase domain with ADP from Thermus thermophilus
Structural highlights
Function[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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedFtsH is a cytoplasmic membrane-integrated, ATP-dependent metalloprotease, which processively degrades both cytoplasmic and membrane proteins in concert with unfolding. The FtsH protein is divided into the N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. We have determined the crystal structures of the Thermus thermophilus FtsH ATPase domain in the nucleotide-free and AMP-PNP- and ADP-bound states, in addition to the domain with the extra preceding segment. Combined with the mapping of the putative substrate binding region, these structures suggest that FtsH internally forms a hexameric ring structure, in which ATP binding could cause a conformational change to facilitate transport of substrates into the protease domain through the central pore. Hexameric ring structure of the ATPase domain of the membrane-integrated metalloprotease FtsH from Thermus thermophilus HB8.,Niwa H, Tsuchiya D, Makyio H, Yoshida M, Morikawa K Structure. 2002 Oct;10(10):1415-23. PMID:12377127[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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