Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
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Journal
IF	>30 >20 >10 >5 all

Title	Ion selectivity and rotor coupling of the Vibrio flagellar sodium-driven stator unit.
Journal, issue, pages	Nat Commun, Vol. 14, Issue 1, Page 4411, Year 2023
Publish date	Jul 27, 2023
Authors	Haidai Hu / Philipp F Popp / Mònica Santiveri / Aritz Roa-Eguiara / Yumeng Yan / Freddie J O Martin / Zheyi Liu / Navish Wadhwa / Yong Wang / Marc Erhardt / Nicholas M I Taylor /
PubMed Abstract	Bacteria swim using a flagellar motor that is powered by stator units. Vibrio spp. are highly motile bacteria responsible for various human diseases, the polar flagella of which are exclusively ...Bacteria swim using a flagellar motor that is powered by stator units. Vibrio spp. are highly motile bacteria responsible for various human diseases, the polar flagella of which are exclusively driven by sodium-dependent stator units (PomAB). However, how ion selectivity is attained, how ion transport triggers the directional rotation of the stator unit, and how the stator unit is incorporated into the flagellar rotor remained largely unclear. Here, we have determined by cryo-electron microscopy the structure of Vibrio PomAB. The electrostatic potential map uncovers sodium binding sites, which together with functional experiments and molecular dynamics simulations, reveal a mechanism for ion translocation and selectivity. Bulky hydrophobic residues from PomA prime PomA for clockwise rotation. We propose that a dynamic helical motif in PomA regulates the distance between PomA subunit cytoplasmic domains, stator unit activation, and torque transmission. Together, our study provides mechanistic insights for understanding ion selectivity and rotor incorporation of the stator unit of the bacterial flagellum.
External links	Nat Commun / PubMed:37500658 / PubMed Central
Methods	EM (single particle)
Resolution	2.48 - 6.3 Å
Structure data	16212 8brd EMDB-16212: VaPomAB_LMNG PDB-8brd: Mechanisms of ion selectivity and rotor coupling in the bacterial flagellar sodium-driven stator unit Method: EM (single particle) / Resolution: 2.48 Å EMDB-16214: VaPomAB full length Saposin Nanodisc Method: EM (single particle) / Resolution: 6.3 Å 16215 8bri EMDB-16215, PDB-8bri: VaPomAB MSP1D1 nanodisc Method: EM (single particle) / Resolution: 3.9 Å
Chemicals	ChemComp-NA: Unknown entry ChemComp-HOH: WATER
Source	vibrio alginolyticus (bacteria)
Keywords	MOTOR PROTEIN / Flagellar sodium-driven stator unit