Structural highlights
Function
GNSA_ECOLI Overexpression increases levels of unsaturated fatty acids and suppresses both the temperature-sensitive fabA6 mutation and cold-sensitive secG null mutation.[1]
Publication Abstract from PubMed
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 A. 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.
Crystal structure of GnsA from Escherichia coli.,Wei Y, Zhan L, Gao Z, Prive GG, Dong Y Biochem Biophys Res Commun. 2015 Jun 19;462(1):1-7. doi:, 10.1016/j.bbrc.2015.03.133. Epub 2015 Apr 1. PMID:25839658[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sugai R, Shimizu H, Nishiyama K, Tokuda H. Overexpression of yccL (gnsA) and ydfY (gnsB) increases levels of unsaturated fatty acids and suppresses both the temperature-sensitive fabA6 mutation and cold-sensitive secG null mutation of Escherichia coli. J Bacteriol. 2001 Oct;183(19):5523-8. PMID:11544213 doi:http://dx.doi.org/10.1128/JB.183.19.5523-5528.2001
- ↑ Wei Y, Zhan L, Gao Z, Prive GG, Dong Y. Crystal structure of GnsA from Escherichia coli. Biochem Biophys Res Commun. 2015 Jun 19;462(1):1-7. doi:, 10.1016/j.bbrc.2015.03.133. Epub 2015 Apr 1. PMID:25839658 doi:http://dx.doi.org/10.1016/j.bbrc.2015.03.133
