4xo1
From Proteopedia
crystal structure of Se-Met GnsA with double mutations
Structural highlights
FunctionGNSA_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 PubMedEscherichia 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
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