Literature DB >> 25839658

Crystal structure of GnsA from Escherichia coli.

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.
Copyright © 2015 Elsevier Inc. All rights reserved.

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


  3 in total

1.  SLING: a tool to search for linked genes in bacterial datasets.

Authors:  Gal Horesh; Alexander Harms; Cinzia Fino; Leopold Parts; Kenn Gerdes; Eva Heinz; Nicholas Robert Thomson
Journal:  Nucleic Acids Res       Date:  2018-11-30       Impact factor: 16.971

2.  A minimal model for gene expression dynamics of bacterial type II toxin-antitoxin systems.

Authors:  Kosmas Kosmidis; Marc-Thorsten Hütt
Journal:  Sci Rep       Date:  2021-09-30       Impact factor: 4.379

3.  Comparative Proteomics Enables Identification of Nonannotated Cold Shock Proteins in E. coli.

Authors:  Nadia G D'Lima; Alexandra Khitun; Aaron D Rosenbloom; Peijia Yuan; Brandon M Gassaway; Karl W Barber; Jesse Rinehart; Sarah A Slavoff
Journal:  J Proteome Res       Date:  2017-09-19       Impact factor: 4.466

  3 in total

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