Open AccessCrystallization and preliminary X‐ray analysis of MotY, a stator component of the Vibrio alginolyticus polar flagellar motor
Author(s) -
Shinohara Akari,
Sakuma Mayuko,
Yakushi Toshiharu,
Kojima Seiji,
Namba Keiichi,
Homma Michio,
Imada Katsumi
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106055850
Subject(s) - vibrio alginolyticus , component (thermodynamics) , stator , crystallization , polar , materials science , physics , chemistry , vibrio , biology , astronomy , bacteria , organic chemistry , genetics , quantum mechanics , thermodynamics
The polar flagellum of Vibrio alginolyticus is rotated by the sodium motor. The stator unit of the sodium motor consists of four different proteins: PomA, PomB, MotX and MotY. MotX and MotY, which are unique components of the sodium motor, form the T‐ring structure attached to the LP ring in the periplasmic space. MotY has a putative peptidoglycan‐binding motif in its C‐terminal region and MotX is suggested to interact with PomB. Thus, MotX and MotY are thought to be required for incorporation and stabilization of the PomA/B complex. In this study, mature MotY composed of 272 amino‐acid residues and its SeMet derivative were expressed with a C‐terminal hexahistidine‐tag sequence, purified and crystallized. Native crystals were grown in the hexagonal space group P 6 1 22/ P 6 5 22, with unit‐cell parameters a = b = 104.1, c = 132.6 Å. SeMet‐derivative crystals belonged to the same space group with the same unit‐cell parameters as the native crystals. Anomalous difference Patterson maps of the SeMet derivative showed significant peaks in their Harker sections, indicating that the derivatives are suitable for structure determination.