5tdy: Difference between revisions
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q9WY64_THEMA Q9WY64_THEMA] The M ring may be actively involved in energy transduction.[PIRNR:PIRNR004862] | [https://www.uniprot.org/uniprot/Q9WY64_THEMA Q9WY64_THEMA] The M ring may be actively involved in energy transduction.[PIRNR:PIRNR004862] | ||
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== 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> | |||
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<div class="pdbe-citations 5tdy" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Flagellar protein 3D structures|Flagellar protein 3D structures]] | *[[Flagellar protein 3D structures|Flagellar protein 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
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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