2ZF8

Crystal structure of MotY

Summary for 2ZF8

• Entry DOI: 10.2210/pdb2zf8/pdb
• Descriptor: Component of sodium-driven polar flagellar motor (2 entities in total)
• Functional Keywords: beta barrel, 2-layer sandwich, flagellum, structural protein
• Biological source: Vibrio alginolyticus
• Total number of polymer chains: 1
• Total formula weight: 32036.13

Authors

Imada, K.,Kojima, S.,Namba, K.,Homma, M. (deposition date: 2007-12-25, release date: 2008-07-08, Last modification date: 2024-10-30)

Primary citation

Kojima, S.,Shinohara, A.,Terashima, H.,Yakushi, T.,Sakuma, M.,Homma, M.,Namba, K.,Imada, K.
Insights into the stator assembly of the Vibrio flagellar motor from the crystal structure of MotY
Proc.Natl.Acad.Sci.Usa, 105:7696-7701, 2008

PubMed Abstract: Rotation of the sodium-driven polar flagellum of Vibrio alginolyticus requires four motor proteins: PomA, PomB, MotX, and MotY. PomA and PomB form a sodium-ion channel in the cytoplasmic membrane that functions as a stator complex to couple sodium-ion flux with torque generation. MotX and MotY are components of the T-ring, which is located beneath the P-ring of the polar flagellar basal body and is involved in incorporation of the PomA/PomB complex into the motor. Here, we describe the determination of the crystal structure of MotY at 2.9 A resolution. The structure shows two distinct domains: an N-terminal domain (MotY-N) and a C-terminal domain (MotY-C). MotY-N has a unique structure. MotY-C contains a putative peptidoglycan-binding motif that is remarkably similar to those of peptidoglycan-binding proteins, such as Pal and RmpM, but this region is disordered in MotY. Motility assay of cells producing either of the MotY-N and MotY-C fragments and subsequent biochemical analyses indicate that MotY-N is essential for association of the stator units around the rotor, whereas MotY-C stabilizes the association by binding to the peptidoglycan layer. Based on these observations, we propose a model for the mechanism of stator assembly around the rotor.

PubMed: 18505842
DOI: 10.1073/pnas.0800308105

Experimental method

X-RAY DIFFRACTION (2.85 Å)