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5VX6

Structure of Bacillus subtilis Inhibitor of motility (MotI/DgrA)

Summary for 5VX6
Entry DOI10.2210/pdb5vx6/pdb
DescriptorUncharacterized protein YpfA, 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one) (2 entities in total)
Functional Keywordsc-di-gmp, ycgr, moti, pilz, dgra, ypfa, motility, gmp binding protein
Biological sourceBacillus subtilis (strain 168)
Total number of polymer chains2
Total formula weight52495.09
Authors
Subramanian, S.,Dann III, C. (deposition date: 2017-05-23, release date: 2017-11-22, Last modification date: 2024-03-13)
Primary citationSubramanian, S.,Gao, X.,Dann 3rd., C.E.,Kearns, D.B.
MotI (DgrA) acts as a molecular clutch on the flagellar stator protein MotA inBacillus subtilis.
Proc. Natl. Acad. Sci. U.S.A., 114:13537-13542, 2017
Cited by
PubMed Abstract: Stator elements consisting of MotAMotB complexes are anchored to the cell wall, extend through the cell membrane, and interact with FliG in the cytoplasmic C ring rotor of the flagellum. The cytoplasmic loop of MotA undergoes proton-driven conformational changes that drive flagellar rotation. Functional regulators inhibit motility by either disengaging or jamming the stator-rotor interaction. Here we show that the YcgR homolog MotI (formerly DgrA) of inhibits motility like a molecular clutch that disengages MotA. MotI-inhibited flagella rotated freely by Brownian motion, and suppressor mutations in MotA that were immune to MotI inhibition were located two residues downstream of the critical force generation site. The 3D structure of MotI bound to c-di-GMP was solved, and MotI-fluorescent fusions localized as transient MotA-dependent puncta at the membrane when induced at subinhibitory levels. Finally, subinhibitory levels of MotI expression resulted in incomplete inhibition and proportional decreases in swimming speed. We propose a model in which flagellar stators are disengaged and sequestered from the flagellar rotor when bound by MotI.
PubMed: 29196522
DOI: 10.1073/pnas.1716231114
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.197 Å)
Structure validation

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