Crystallization and preliminary X-ray analysis of MotY, a stator component of the Vibrio alginolyticus polar flagellar motor

Journal Article · Thu Feb 01 04:00:00 EST 2007 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309106055850· OSTI ID:22360255

Shinohara, Akari ^[1]; Sakuma, Mayuko ^[2]; Yakushi, Toshiharu ^[1]; Kojima, Seiji ^[2]; Namba, Keiichi ^[3]; Homma, Michio ^[1]; Imada, Katsumi ^[3]

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1. Soft Nano-Machine Project, CREST, JST, Chikusa-ku, Nagoya 464-8602 (Japan)
2. Division of Biological Science, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-8602 (Japan)
3. Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871 (Japan)

Crystals of MotY, a stator protein of the V. alginolyticus polar flagellar motor, have been produced and characterized by X-ray diffraction. 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 P6{sub 1}22/P6{sub 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.

• OSTI ID: 22360255
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 2 Vol. 63; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
CRYSTALS
PEAKS
PROTEINS
RINGS
SODIUM
SPACE GROUPS
STABILIZATION
STATORS
X-RAY DIFFRACTION