5tdy: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TDY FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tdy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tdy OCA], [http://pdbe.org/5tdy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tdy RCSB], [http://www.ebi.ac.uk/pdbsum/5tdy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tdy ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/Q9WY64_THEMA Q9WY64_THEMA]] The M ring may be actively involved in energy transduction.[PIRNR:PIRNR004862] [[http://www.uniprot.org/uniprot/FLIG_THEMA FLIG_THEMA]] One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity). | |||
<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> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Blair, D F]] | |||
[[Category: Crane, B R]] | |||
[[Category: Dahlquist, F W]] | |||
[[Category: Kim, E A]] | |||
[[Category: Levenson, R]] | |||
[[Category: Lynch, M J]] | |||
[[Category: Sircar, R]] | |||
[[Category: Flagellar motor]] | |||
[[Category: Motor protein]] | |||
[[Category: Switch complex]] | |||
Revision as of 02:34, 26 January 2017
Structure of cofolded FliFc:FliGn complex from Thermotoga maritimaStructure of cofolded FliFc:FliGn complex from Thermotoga maritima
Structural highlights
Function[Q9WY64_THEMA] The M ring may be actively involved in energy transduction.[PIRNR:PIRNR004862] [FLIG_THEMA] One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity). 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. References
|
| ||||||||||||||||