7wi4
From Proteopedia
(Difference between revisions)
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==Cryo-EM structure of E.Coli FtsH protease cytosolic domains== | ==Cryo-EM structure of E.Coli FtsH protease cytosolic domains== | ||
| - | <StructureSection load='7wi4' size='340' side='right'caption='[[7wi4]]' scene=''> | + | <StructureSection load='7wi4' size='340' side='right'caption='[[7wi4]], [[Resolution|resolution]] 3.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WI4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WI4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7wi4]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WI4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WI4 FirstGlance]. <br> |
| - | </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=7wi4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wi4 OCA], [https://pdbe.org/7wi4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wi4 RCSB], [https://www.ebi.ac.uk/pdbsum/7wi4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wi4 ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7wi4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wi4 OCA], [https://pdbe.org/7wi4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wi4 RCSB], [https://www.ebi.ac.uk/pdbsum/7wi4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wi4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/FTSH_ECOLI FTSH_ECOLI]] 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. Degrades a few membrane proteins that have not been assembled into complexes such as SecY, F(0) ATPase subunit a and YccA, and also cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein among others. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent sequence requirements. It presumably dislocates membrane-spanning and periplasmic segments of the protein into the cytoplasm to degrade them, this probably requires ATP. Degrades C-terminal-tagged cytoplasmic proteins which are tagged with an 11-amino-acid nonpolar destabilizing tail via a mechanism involving the 10SA (SsrA) stable RNA.<ref>PMID:7781608</ref> <ref>PMID:7753838</ref> <ref>PMID:10048027</ref> <ref>PMID:18776015</ref> As FtsH regulates the levels of both LpxC and KdtA it is required for synthesis of both the protein and lipid components of lipopolysaccharide (LPS).<ref>PMID:7781608</ref> <ref>PMID:7753838</ref> <ref>PMID:10048027</ref> <ref>PMID:18776015</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The membrane-bound AAA protease FtsH is the key player controlling protein quality in bacteria. Two single-pass membrane proteins, HflK and HflC, interact with FtsH to modulate its proteolytic activity. Here, we present structure of the entire FtsH-HflKC complex, comprising 12 copies of both HflK and HflC, all of which interact reciprocally to form a cage, as well as four FtsH hexamers with periplasmic domains and transmembrane helices enclosed inside the cage and cytoplasmic domains situated at the base of the cage. FtsH K61/D62/S63 in the beta2-beta3 loop in the periplasmic domain directly interact with HflK, contributing to complex formation. Pull-down and in vivo enzymatic activity assays validate the importance of the interacting interface for FtsH-HflKC complex formation. Structural comparison with the substrate-bound human m-AAA protease AFG3L2 offers implications for the HflKC cage in modulating substrate access to FtsH. Together, our findings provide a better understanding of FtsH-type AAA protease holoenzyme assembly and regulation. | ||
| + | |||
| + | Cryo-EM structure of the entire FtsH-HflKC AAA protease complex.,Qiao Z, Yokoyama T, Yan XF, Beh IT, Shi J, Basak S, Akiyama Y, Gao YG Cell Rep. 2022 May 31;39(9):110890. doi: 10.1016/j.celrep.2022.110890. PMID:35649372<ref>PMID:35649372</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7wi4" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Gao | + | [[Category: Gao, Y G]] |
| - | [[Category: Qiao Z]] | + | [[Category: Qiao, Z]] |
| + | [[Category: Complex]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Membrane protein]] | ||
Current revision
Cryo-EM structure of E.Coli FtsH protease cytosolic domains
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