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Acta Crystallogr F Struct Biol Commun. 2014 Sep;70(Pt 9):1260-3. doi: 10.1107/S2053230X14017397. Epub 2014 Aug 27.

Purification, crystallization and preliminary X-ray crystallographic analysis of TssL from Vibrio cholerae.

Author information

1
Beamline Science Division, Pohang Accelerator Laboratory, Jigok-ro 127, Pohang 790-784, Republic of Korea.
2
Department of Biology, Teachers College, Kyungpook National University, Daehak-ro 80, Buk-ku, Daegu 702-701, Republic of Korea.

Abstract

The type VI secretion system (T6SS) is a macromolecular complex that is conserved in Gram-negative bacteria. The T6SS secretes effector proteins into recipient cells in a contact-dependent manner in order to accomplish cooperative and competitive interactions with the cells. Although the composition and mechanism of the T6SS have been intensively investigated across many Gram-negative bacteria, to date structural information on T6SS components from the important pathogen Vibrio cholerae has been rare. Here, the cloning, purification, crystallization and preliminary X-ray crystallographic analysis of the cytoplasmic domain of TssL, an inner membrane protein of the T6SS, from V. cholerae are reported. Diffraction data were collected to 1.5 Å resolution using synchrotron radiation. The crystal belonged to the hexagonal space group P61, with unit-cell parameters a = 78.4, b = 78.4, c = 49.5 Å. The successful structural characterization of TssL from V. cholerae will contribute to understanding the role of the membrane-associated subunits of the T6SS in more detail.

KEYWORDS:

T6SS; TssL; Vibrio cholerae

PMID:
25195905
PMCID:
PMC4157432
DOI:
10.1107/S2053230X14017397
[Indexed for MEDLINE]
Free PMC Article

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