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Purification, crystallization and preliminary X-ray crystallographic analysis of TssL from Vibrio cholerae.
- Source :
-
Acta Crystallographica: Section F, Structural Biology Communications . Sep2014, Vol. 70 Issue 9, p1260-1263. 4p. - Publication Year :
- 2014
-
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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 2053230X
- Volume :
- 70
- Issue :
- 9
- Database :
- Academic Search Index
- Journal :
- Acta Crystallographica: Section F, Structural Biology Communications
- Publication Type :
- Academic Journal
- Accession number :
- 97983133
- Full Text :
- https://doi.org/10.1107/S2053230X14017397