4XO2

crystal structure of GnsA from E.coli

Summary for 4XO2

• Entry DOI: 10.2210/pdb4xo2/pdb
• Related: 4XO1
• Descriptor: Protein GnsA (2 entities in total)
• Functional Keywords: suppressor, protein binding
• Biological source: Escherichia coli (strain K12)
• Total number of polymer chains: 2
• Total formula weight: 13932.07

Authors

Zhan, L.H.,Gao, Z.Q.,Wei, Y.,Dong, Y.H. (deposition date: 2015-01-16, release date: 2015-06-17, Last modification date: 2024-03-20)

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

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

Experimental method

X-RAY DIFFRACTION (1.952 Å)