title: Crystal structure of GnsA from Escherichia coli.
abstract: Escherichia Coli GnsA is a regulator of phosphatidylethanolamine synthesis and functions as a suppressor of both a secG null mutation and fabA6 mutations. GnsA may also be a toxin with the cognate antitoxin YmcE. Here we report the crystal structure of GnsA to 1.8 Å. GnsA forms a V shaped hairpin structure that is tightly associated into a homodimer. Our comprehensive structural study suggests that GnsA is structurally similar to an outer membrane protein, suggesting a function of protein binding.
authors.affiliation: School of Life Science, University of Science and Technology of China, Hefei 230027, China; Department of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada. Electronic address: yongwei@uhnresearch.ca.
authors.forename: Yong
authors.initials: Y
authors.lastname: Wei
authors.affiliation: School of Life Science, University of Science and Technology of China, Hefei 230027, China; Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, China.
authors.forename: Lihong
authors.initials: L
authors.lastname: Zhan
authors.affiliation: Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, China.
authors.forename: Zengqiang
authors.initials: Z
authors.lastname: Gao
authors.affiliation: Department of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada; Princess Margaret Cancer Centre, Toronto, Ontario, Canada. Electronic address: prive@uhnresearch.ca.
authors.forename: Gilbert G
authors.initials: GG
authors.lastname: Privé
authors.affiliation: Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, China. Electronic address: dongyh@ihep.ac.cn.
authors.forename: Yuhui
authors.initials: Y
authors.lastname: Dong
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D011485:Protein Binding; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D029968:Escherichia coli Proteins; C490218:GnsA protein, E coli
keywords: Crystal structure; PE synthesis; Site-directed mutagenesis; Toxin-antitoxin