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Author Shinohara, Akari ♦ Sakuma, Mayuko ♦ Yakushi, Toshiharu ♦ Kojima, Seiji ♦ Namba, Keiichi ♦ Homma, Michio ♦ Imada, Katsumi
Source World Health Organization (WHO)-Global Index Medicus
Content type Text
Publisher Wiley
File Format HTM / HTML
Language English
Difficulty Level Medium
Subject Domain (in DDC) Natural sciences & mathematics ♦ Chemistry & allied sciences ♦ Crystallography ♦ Life sciences; biology ♦ Biochemistry ♦ Natural history of organisms ♦ Microorganisms, fungi & algae ♦ Technology ♦ Medicine & health ♦ Human anatomy, cytology, histology ♦ Pharmacology and therapeutics ♦ Diseases ♦ Manufacture for specific uses ♦ Precision instruments & other devices
Subject Domain (in MeSH) Cells ♦ Anatomy ♦ Bacteria ♦ Organisms ♦ Macromolecular Substances ♦ Amino Acids, Peptides, and Proteins ♦ Chemicals and Drugs ♦ Investigative Techniques ♦ Analytical, Diagnostic and Therapeutic Techniques and Equipment
Subject Keyword Discipline Crystallography ♦ Discipline Biophysics ♦ Discipline Molecular Biology ♦ Discipline Biochemistry ♦ Bacterial Outer Membrane Proteins ♦ Chemistry ♦ Molecular Motor Proteins ♦ Vibrio Alginolyticus ♦ Biosynthesis ♦ Genetics ♦ Crystallization ♦ Crystallography, X-ray ♦ Escherichia Coli ♦ Metabolism ♦ Flagella ♦ Journal Article ♦ Research Support, Non-u.s. Gov't
Abstract 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(1)22/P6(5)22, with unit-cell parameters a = b = 104.1, c = 132.6 A. 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.
Description Country affiliation: Japan
Author Affiliation: Shinohara A ( Soft Nano-Machine Project, CREST, JST, Chikusa-ku, Nagoya 464-8602, Japan.)
ISSN 2053230X
Educational Role Student ♦ Teacher
Age Range above 22 year
Educational Use Reading ♦ Research ♦ Self Learning
Interactivity Type Expositive
Education Level UG and PG
Learning Resource Type Article
Publisher Date 2007-02-01
Publisher Place Great Britain (UK)
e-ISSN 17443091
Journal Acta Crystallographica Section F Structural Biology and Crystallization Communications
Volume Number 63
Issue Number Pt 2


Source: WHO-Global Index Medicus