View source for 5tdy


==Structure of cofolded FliFc:FliGn complex from Thermotoga maritima==
<StructureSection load='5tdy' size='340' side='right'caption='[[5tdy]], [[Resolution|resolution]] 2.10&Aring;' 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]] 2.105&#8491;</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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</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]]