A new algorithm for particle weighted subtraction to decrease signals from unwanted components in single particle analysis

Fernández-Giménez, E.; Martínez, M.M.; Marabini, R.; Strelak, D.; Sánchez-García, R.; Carazo, J.M.; Sorzano, C.O.S.

doi:10.1016/j.jsb.2023.108024

Cited by 1 publication

(1 citation statement)

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“…1a ). This technique improves alignment by obscuring unwanted features in the primary dataset 28 , with common applications including removing nanodiscs or detergent micelles from membrane protein particles. We removed the MS-ring and determined the structure of the C-ring, where the predominant species was a 34-mer (~50% of the particles).…”

Section: Resultsmentioning

confidence: 99%

CryoEM structures reveal how the bacterial flagellum rotates and switches direction

Singh,

Sharma,

Afanzar

et al. 2024

Nat Microbiol

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Bacterial chemotaxis requires bidirectional flagellar rotation at different rates. Rotation is driven by a flagellar motor, which is a supercomplex containing multiple rings. Architectural uncertainty regarding the cytoplasmic C-ring, or ‘switch’, limits our understanding of how the motor transmits torque and direction to the flagellar rod. Here we report cryogenic electron microscopy structures for Salmonella enterica serovar typhimurium inner membrane MS-ring and C-ring in a counterclockwise pose (4.0 Å) and isolated C-ring in a clockwise pose alone (4.6 Å) and bound to a regulator (5.9 Å). Conformational differences between rotational poses include a 180° shift in FliF/FliG domains that rotates the outward-facing MotA/B binding site to inward facing. The regulator has specificity for the clockwise pose by bridging elements unique to this conformation. We used these structures to propose how the switch reverses rotation and transmits torque to the flagellum, which advances the understanding of bacterial chemotaxis and bidirectional motor rotation.

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Section: Resultsmentioning

confidence: 99%