5tdy: Difference between revisions
New page: '''Unreleased structure''' The entry 5tdy is ON HOLD Authors: Description: Category: Unreleased Structures |
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The | ==Structure of cofolded FliFc:FliGn complex from Thermotoga maritima== | ||
<StructureSection load='5tdy' size='340' side='right'caption='[[5tdy]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5tdy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TDY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TDY FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.105Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5tdy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tdy OCA], [https://pdbe.org/5tdy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tdy RCSB], [https://www.ebi.ac.uk/pdbsum/5tdy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tdy ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9WY64_THEMA Q9WY64_THEMA] The M ring may be actively involved in energy transduction.[PIRNR:PIRNR004862] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The interface between the membrane (MS) and cytoplasmic (C) rings of the bacterial flagellar motor couples torque generation to rotation within the membrane. The structure of the C-terminal helices of the integral membrane protein FliF (FliFC) bound to the N terminal domain of the switch complex protein FliG (FliGN) reveals that FliGN folds around FliFC to produce a topology that closely resembles both the middle and C-terminal domains of FliG. The interface is consistent with solution-state nuclear magnetic resonance, small-angle X-ray scattering, in vivo interaction studies, and cellular motility assays. Co-folding with FliFC induces substantial conformational changes in FliGN and suggests that FliF and FliG have the same stoichiometry within the rotor. Modeling the FliFC:FliGN complex into cryo-electron microscopy rotor density updates the architecture of the middle and upper switch complex and shows how domain shuffling of a conserved interaction module anchors the cytoplasmic rotor to the membrane. | |||
Co-Folding of a FliF-FliG Split Domain Forms the Basis of the MS:C Ring Interface within the Bacterial Flagellar Motor.,Lynch MJ, Levenson R, Kim EA, Sircar R, Blair DF, Dahlquist FW, Crane BR Structure. 2016 Dec 31. pii: S0969-2126(16)30396-3. doi:, 10.1016/j.str.2016.12.006. PMID:28089452<ref>PMID:28089452</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5tdy" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Flagellar protein 3D structures|Flagellar protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermotoga maritima MSB8]] | |||
[[Category: Blair DF]] | |||
[[Category: Crane BR]] | |||
[[Category: Dahlquist FW]] | |||
[[Category: Kim EA]] | |||
[[Category: Levenson R]] | |||
[[Category: Lynch MJ]] | |||
[[Category: Sircar R]] | |||
Latest revision as of 07:42, 21 November 2024
Structure of cofolded FliFc:FliGn complex from Thermotoga maritimaStructure of cofolded FliFc:FliGn complex from Thermotoga maritima
Structural highlights
FunctionQ9WY64_THEMA The M ring may be actively involved in energy transduction.[PIRNR:PIRNR004862] Publication Abstract from PubMedThe interface between the membrane (MS) and cytoplasmic (C) rings of the bacterial flagellar motor couples torque generation to rotation within the membrane. The structure of the C-terminal helices of the integral membrane protein FliF (FliFC) bound to the N terminal domain of the switch complex protein FliG (FliGN) reveals that FliGN folds around FliFC to produce a topology that closely resembles both the middle and C-terminal domains of FliG. The interface is consistent with solution-state nuclear magnetic resonance, small-angle X-ray scattering, in vivo interaction studies, and cellular motility assays. Co-folding with FliFC induces substantial conformational changes in FliGN and suggests that FliF and FliG have the same stoichiometry within the rotor. Modeling the FliFC:FliGN complex into cryo-electron microscopy rotor density updates the architecture of the middle and upper switch complex and shows how domain shuffling of a conserved interaction module anchors the cytoplasmic rotor to the membrane. Co-Folding of a FliF-FliG Split Domain Forms the Basis of the MS:C Ring Interface within the Bacterial Flagellar Motor.,Lynch MJ, Levenson R, Kim EA, Sircar R, Blair DF, Dahlquist FW, Crane BR Structure. 2016 Dec 31. pii: S0969-2126(16)30396-3. doi:, 10.1016/j.str.2016.12.006. PMID:28089452[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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