Browse > Article

Crystallization and Preliminary X-Ray Crystallographic Analysis of PAS Factor from Vibrio vulnificus  

Lee, Jun Hyuck (Department of Life Science, Gwangju Institute of Science and Technology)
Kim, Soo Young (Department of Microbiology, Chonnam National University Medical School)
Rho, Seong-Hwan (Department of Life Science, Gwangju Institute of Science and Technology)
Im, Young Jun (Department of Life Science, Gwangju Institute of Science and Technology)
Kim, Young Ran (Department of Microbiology, Chonnam National University Medical School)
Kim, Mun-Kyoung (Department of Life Science, Gwangju Institute of Science and Technology)
Kang, Gil Bu (Department of Life Science, Gwangju Institute of Science and Technology)
Rhee, Joon Haeng (Department of Microbiology, Chonnam National University Medical School)
Eom, Soo Hyun (Department of Life Science, Gwangju Institute of Science and Technology)
Publication Information
Molecules and Cells / v.20, no.3, 2005 , pp. 361-363 More about this Journal
Abstract
Plasmid Achromobacter secretion (PAS) factor is a putative secretion factor that induces the secretion of periplasmic proteins. PAS factor from Vibrio vulnificus was crystallized at 294 K by the hanging drop vapor-diffusion method. It was isolated as a monomer during the purification procedures. The native crystal belongs to the F222 space group with unit cell parameters a = 56.1, b = 74.4, $c=80.0{\AA}$, ${\alpha}={\beta}={\gamma}=90^{\circ}$. The crystal was soaked in cryoprotectant containing 1 M NaBr for 1 h for MAD phasing. The diffraction limit of the Br-MAD data set was $1.9{\AA}$ using synchrotron X-ray irradiation at beam line BL-18B at the Photon Factory, Japan.
Keywords
PAS Factor; Secretion; Vibrio vulnificus; X-Ray Crystallography;
Citations & Related Records
Times Cited By KSCI : 2  (Citation Analysis)
Times Cited By Web Of Science : 1  (Related Records In Web of Science)
연도 인용수 순위
1 Finlay, B. B. and Falkow, S. (1997) Common themes in microbial pathogenicity revisited. Microbiol. Mol. Biol. Rev. 61, 136-169
2 Gray, L. D. and Kreger, A. S. (1989) Detection of Vibrio vulnificus cytolysin in V. vulnificus-infected mice. Toxicon 27, 439-464   DOI   ScienceOn
3 Jeong, M. S. and Jang, S. B. (2005) Crystallization and X-ray crystallographic studies of wild-type and mutant tryptophan synthase ${\alpha}$ -subunits from Escherichia coli. Mol. Cells 19, 219-222
4 Kreger, A., DeChatelet, L., and Shirley, P. (1981) Interaction of Vibrio vulnificus with human polymorphonuclear leukocytes: association of virulence with resistance to phagocytosis. J. Infect. Dis. 144, 244-248   DOI   ScienceOn
5 Morris, J. G. Jr., Wright, A. C., Simpson, L. M., Wood, P. K., Johnson, D. E., et al. (1987) Virulence of Vibrio vulnificus: association with utilization of transferrin-bound iron, and lack of correlation with levels of cytotoxin or protease production. FEMS Microbiol. Lett. 40, 55-59   DOI   ScienceOn
6 Tokugawa, K., Kakitani, M., Ishii, T., Nakamura, K., Masaki, H., et al. (1994a) A novel protein secretion factor from a Vibrio species which operates in Escherichia coli. J. Biotechnol. 35, 69-76   DOI   ScienceOn
7 Hampel, A., Labanauskas, M., Connor, P. G., Kirkegard, L., RajBhandary, U. L., et al. (1968) Single crystals of transfer RNA from formylmethionine and phenylalanine transfer RNA's. Science 162, 1384-1387   DOI   ScienceOn
8 Tokugawa, K., Ishii, T., Nakamura, K., Masaki, H., and Uozumi, T. (1994b) A model system for the continuous production of a heterologous protein using a novel secretion promoting factor which operates in Escherichia coli. J. Biotechnol. 37, 33-37   DOI   ScienceOn
9 Wright, A. L., Miceli, G. A., Landry, W. L., Christy, J. B., Watkins, W. D., et al. (1993) Rapid identification of Vibrio vulnificus on nonselective media with an alkaline phosphataselabeled oligonucleotide probe. Appl. Environ. Microbiol. 59, 541-546
10 Miroux, B. and Walker, J. E. (1996) Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260, 289-298   DOI   ScienceOn
11 Matthews, B. W. (1968) Solvent content of protein crystals. J. Mol. Biol. 33, 491-497   DOI
12 Oliver, J. D., Wear, J. E., Thomas, M. B., Warner, M., and Linder, K. (1986) Production of extracellular enzymes and cytotoxicity by Vibrio vulnificus. Diagn. Microbiol. Infect. Dis. 5, 99-111   DOI   ScienceOn
13 Terwilliger, T. C. (1999) Reciprocal-space solvent flattening. Acta Cryst. D55, 1863-1871
14 McPherson, V. L., Watts, J. A., Simpson, L. M., and Oliver, J. D. (1991) Physiological effects of the lipopolysaccharide of Vibrio vulnificus on mice and rats. Microbios 67, 141-149
15 Terwilliger, T. C. and Berendzen, J. (1999) Automated MAD and MIR structure solution. Acta Cryst. D55, 849-861
16 Otwinowsky, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326   DOI
17 Simpson, L. M. and Oliver, J. D. (1987) Ability of Vibrio vulnificus to obtain iron from transferrin and other iron-binding proteins. Curr. Microbiol. 15, 155-157   DOI
18 Kim, Y. R., Lee, S. E., Kim, C. M., Kim, S. Y., Shin, E. K., et al. (2003) Characterization and pathogenic significance of Vibrio vulnificus antigens preferentially expressed in septicemic patients. Infect. Immun. 71, 5461-5471   DOI