4XO1

crystal structure of Se-Met GnsA with double mutations

Summary for 4XO1

Entry DOI	10.2210/pdb4xo1/pdb
Related	4XO2
Descriptor	Protein GnsA (2 entities in total)
Functional Keywords	suppressor, protein binding
Biological source	Escherichia coli
Total number of polymer chains	1
Total formula weight	7236.59
Authors	Zhan, L.,Gao, Z.,Dong, Y. (deposition date: 2015-01-16, release date: 2015-07-29, Last modification date: 2024-10-30)
Primary citation	Wei, Y.,Zhan, L.,Gao, Z.,Prive, G.G.,Dong, Y. Crystal structure of GnsA from Escherichia coli Biochem.Biophys.Res.Commun., 462:1-7, 2015 Cited by PubMed 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. PubMed: 25839658 DOI: 10.1016/j.bbrc.2015.03.133 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.802 Å)

Structure validation