| Literature DB >> 25839658 |
Yong Wei1, Lihong Zhan2, Zengqiang Gao3, Gilbert G Privé4, Yuhui Dong5.
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.Entities:
Keywords: Crystal structure; PE synthesis; Site-directed mutagenesis; Toxin-antitoxin
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Year: 2015 PMID: 25839658 DOI: 10.1016/j.bbrc.2015.03.133
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575