Title | Crystallization and preliminary X-ray study of TsiV3 from Vibrio cholerae |
Authors | Zhang, Jiulong Zhang, Heng Liu, Ying Zhan, Lihong She, Zhun Dong, Cheng Dong, Yuhui |
Affiliation | Univ Sci & Technol China, Sch Life Sci, Anhua 230026, Peoples R China. Peking Univ, Sch Life Sci, State Key Lab Prot & Plant Gene Res, Beijing 100871, Peoples R China. Chinese Acad Sci, Inst High Energy Phys, Beijing Synchrotron Radiat Facil, Beijing 100049, Peoples R China. Nankai Univ, State Key Lab Med Chem Biol, Tianjin 300071, Peoples R China. |
Keywords | IMMUNITY PROTEIN SECRETION-SYSTEM TARGET-CELLS EFFECTOR IDENTIFICATION INHIBITION INSIGHTS SPIKE |
Issue Date | 2014 |
Publisher | acta crystallographica section f structural biology and crystallization communications |
Citation | ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS.2014,70,335-338. |
Abstract | The bacterial type VI secretion system (T6SS), a dynamic organelle, participates in microbial competition by transporting toxic effector molecules to neighbouring cells to kill competitors. TsiV3, a recently defined T6SS immunity protein in Vibrio cholerae, possesses self-protection against killing by T6SS predatory cells by directly binding to and inhibiting their effector protein VgrG-3. Structural information about TsiV3 could help to illuminate its specific mechanism. In this study, TsiV3 from V. cholerae was cloned, expressed and crystallized and single-crystal X-ray diffraction data sets were collected to a resolution of 2.55 angstrom. Specifically, the crystal belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 73.3, b = 78.12, c = 106.18 angstrom. Matthews coefficient calculations indicated that the crystal may contain six TsiV3 molecules in one asymmetric unit, with a V-M value of 2.25 angstrom(3) Da(-1) and a solvent content of 45.42%. |
URI | http://hdl.handle.net/20.500.11897/342356 |
ISSN | 1744-3091 |
DOI | 10.1107/S2053230X14001599 |
Indexed | SCI(E) PubMed |
Appears in Collections: | 生命科学学院 |