2ZVZ

Structure of the periplasmic domain of MotB from Salmonella (crystal form III)

Summary for 2ZVZ

• Entry DOI: 10.2210/pdb2zvz/pdb
• Related: 2zov 2zvy
• Descriptor: Chemotaxis protein motB (2 entities in total)
• Functional Keywords: 2-layer sandwich, bacterial flagellum, cell inner membrane, cell membrane, chemotaxis, flagellar rotation, membrane, transmembrane, membrane protein
• Biological source: Salmonella typhimurium
• Cellular location: Cell inner membrane (By similarity); Single- pass type II membrane protein (Potential): P55892
• Total number of polymer chains: 2
• Total formula weight: 41469.34

Authors

Imada, K.,Kojima, S.,Namba, K.,Homma, S. (deposition date: 2008-11-26, release date: 2009-09-01, Last modification date: 2023-11-01)

Primary citation

Kojima, S.,Imada, K.,Sakuma, M.,Sudo, Y.,Kojima, C.,Minamino, T.,Homma, M.,Namba, K.
Stator assembly and activation mechanism of the flagellar motor by the periplasmic region of MotB
Mol.Microbiol., 73:710-718, 2009

PubMed Abstract: Torque generation in the Salmonella flagellar motor is coupled to translocation of H(+) ions through the proton-conducting channel of the Mot protein stator complex. The Mot complex is believed to be anchored to the peptidoglycan (PG) layer by the putative peptidoglycan-binding (PGB) domain of MotB. Proton translocation is activated only when the stator is installed into the motor. We report the crystal structure of a C-terminal periplasmic fragment of MotB (MotB(C)) that contains the PGB domain and includes the entire periplasmic region essential for motility. Structural and functional analyses indicate that the PGB domains must dimerize in order to form the proton-conducting channel. Drastic conformational changes in the N-terminal portion of MotB(C) are required both for PG binding and the proton channel activation.

PubMed: 19627504
DOI: 10.1111/j.1365-2958.2009.06802.x

Experimental method

X-RAY DIFFRACTION (2.4 Å)