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
Author
Journal
IF	>30 >20 >10 >5 all

Title	Molecular basis of high-torque transmission of the Vibrio polar flagellar motor.
Journal, issue, pages	Protein Cell, Year 2026
Publish date	Mar 23, 2026
Authors	Ling Zhang / Jiaxing Tan / Xuemin Duan / Xiaofei Wang / Ting Wang / Keke Yuan / Michio Homma / Seiji Kojima / Yan Zhou / Yongqun Zhu /
PubMed Abstract	The bacterial flagellar motor is a protein nanomachine that rotates the flagellum to facilitate bacterial motility. These motors exhibit structural diversity among species, enabling the transmission ...The bacterial flagellar motor is a protein nanomachine that rotates the flagellum to facilitate bacterial motility. These motors exhibit structural diversity among species, enabling the transmission of varying torques to flagellar filaments to grant bacteria diverse swimming capabilities. Compared to peritrichous flagellar motors, polar flagellar motors are faster machines that transmit higher torque to drive high-speed motility in liquids and empower swimming in viscous environments. However, structural basis of high-torque transmission of the polar flagellar motors is still unclear. Here we present a cryo-electron microscopy structure of the polar flagellar motor in complex with the hook from Vibrio alginolyticus, comprising 295 subunits from 18 proteins. Compared to the peritrichous flagellar rod, this structure reveals an increased number of inter-subunit interactions in the rod of the polar flagellar motor. Nine phospholipid molecules insert into the interface between the export apparatus and the proximal rod. The LP ring contains more electrostatic charges on the inner surface and has fewer physical contacts with the rod, while the HT ring tightly binds to the outer surface of the LP ring. FlrP, a protein of previously unknown function, is identified as a new component of the polar flagellar motor, and extensively participates in the interactions of 15 FliF peptides of the MS ring with the rod. In contrast to that in the peritrichous flagellum, the hook in the polar flagellum has two different conformational states, L- and R-types. These findings provide unprecedented insights into structural adaptations of the bacterial polar flagellar motors for high-torque transmission.
External links	Protein Cell / PubMed:41871453
Methods	EM (single particle)
Resolution	2.93 - 3.64 Å
Structure data	39776 8z5n EMDB-39776, PDB-8z5n: Cryo-EM structure of the LPHT ring Method: EM (single particle) / Resolution: 2.95 Å 39780 8z5s EMDB-39780, PDB-8z5s: Cryo-EM structure of the proximal rod-export apparatus of the polar flagellar motor Method: EM (single particle) / Resolution: 3.03 Å 39782 8z5u EMDB-39782, PDB-8z5u: Cryo-EM structure of the rod-export apparatus with partial hook within the polar flagellar motor Method: EM (single particle) / Resolution: 3.04 Å 39783 8z5v EMDB-39783, PDB-8z5v: Cryo-EM structure of the MS ring (C34) within the polar flagellar motor Method: EM (single particle) / Resolution: 2.93 Å 39786 8z5w EMDB-39786, PDB-8z5w: Cryo-EM structure of the LRR protein within the polar flagellar motor Method: EM (single particle) / Resolution: 3.46 Å 39787 8z5x EMDB-39787, PDB-8z5x: Cryo-EM structure of the MS ring with the proximal rod and the export apparatus (C1) within the polar flagellar motor Method: EM (single particle) / Resolution: 3.64 Å 39788 8z5y EMDB-39788, PDB-8z5y: Cryo-EM structure of the L-hook of the polar flagellum Method: EM (single particle) / Resolution: 3.22 Å 39789 8z5z EMDB-39789, PDB-8z5z: Cryo-EM structure of the R-hook of the polar flagellum Method: EM (single particle) / Resolution: 3.42 Å 39790 8z60 EMDB-39790, PDB-8z60: Cryo-EM structure of the polar flagellar motor-hook complex Method: EM (single particle) / Resolution: 3.22 Å
Chemicals	ChemComp-PGT: (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE / phospholipidYM ChemComp-XKP*: (11R,14S)-17-amino-14-hydroxy-8,14-dioxo-9,13,15-trioxa-14lambda~5~-phosphaheptadecan-11-yl decanoate
Source	vibrio alginolyticus (bacteria)
Keywords	MOTOR PROTEIN / Polar flagellum / Polar flagellar motor / LPHT ring / Bushing / Proximal rod / Rod / MS ring / LRR / Hook