5Y3Z

Structure of the periplasmic domain of the MotB L119P mutant from Salmonella (crystal form 1)

Summary for 5Y3Z

• Entry DOI: 10.2210/pdb5y3z/pdb
• Related: 2ZOV 2ZVY 2ZVZ
• Descriptor: Motility protein B, ARGININE, IMIDAZOLE, ... (5 entities in total)
• Functional Keywords: 2-layer sandwich, bacterial flagellum, cell projection, chemotaxis, flagellar rotation, inner membrane, membrane protein, motor protein
• Biological source: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
• Cellular location: Cell inner membrane ; Single- pass type II membrane protein : P55892
• Total number of polymer chains: 2
• Total formula weight: 42455.58

Authors

Takao, M.,Kojima, S.,Sakuma, M.,Homma, M.,Imada, K. (deposition date: 2017-07-31, release date: 2018-04-11, Last modification date: 2023-11-22)

Primary citation

Kojima, S.,Takao, M.,Almira, G.,Kawahara, I.,Sakuma, M.,Homma, M.,Kojima, C.,Imada, K.
The Helix Rearrangement in the Periplasmic Domain of the Flagellar Stator B Subunit Activates Peptidoglycan Binding and Ion Influx.
Structure, 26:590-598.e5, 2018

PubMed Abstract: The stator of the bacterial flagellar motor couples ion flow with torque generation. The ion-conducting stator channel opens only when incorporated into and anchored around the rotor via the peptidoglycan (PG) binding domain of the B subunit (MotB). However, no direct evidence of PG binding coupled with channel activation has been presented. Here, we report the structural rearrangements of MotB responsible for this coupling process. A MotB fragment with the L119P replacement, which is known to cause channel activation, was able to bind PG. Nuclear magnetic resonance analysis of MotB and the crystal structure of the MotB-L119P dimer revealed major structural changes in helix α1. In vivo crosslinking results confirm that a major rearrangement occurs. Our results suggest that, upon stator incorporation into the motor, helix α1 of MotB changes into an extended non-helical structure. We propose that this change allows the stator both to bind PG and to open its proton channel.

PubMed: 29576320
DOI: 10.1016/j.str.2018.02.016

Experimental method

X-RAY DIFFRACTION (2 Å)