3G1Z

Structure of IDP01693/yjeA, a potential t-RNA synthetase from Salmonella typhimurium

Summary for 3G1Z

• Entry DOI: 10.2210/pdb3g1z/pdb
• Descriptor: Putative lysyl-tRNA synthetase, ADENOSINE MONOPHOSPHATE, PHOSPHATE ION, ... (5 entities in total)
• Functional Keywords: t-rna synthetase, drug target, salmonella typhimurium, nucleotide, aminoacyl-trna synthetase, atp-binding, ligase, nucleotide-binding, protein biosynthesis, structural genomics, center for structural genomics of infectious diseases, csgid
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 2
• Total formula weight: 75209.27

Authors

Singer, A.U.,Evdokimova, E.,Kudritska, M.,Cuff, M.E.,Edwards, A.M.,Anderson, W.F.,Savchenko, A.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2009-01-30, release date: 2009-03-10, Last modification date: 2024-04-03)

Primary citation

Navarre, W.W.,Zou, S.B.,Roy, H.,Xie, J.L.,Savchenko, A.,Singer, A.,Edvokimova, E.,Prost, L.R.,Kumar, R.,Ibba, M.,Fang, F.C.
PoxA, yjeK, and elongation factor P coordinately modulate virulence and drug resistance in Salmonella enterica.
Mol.Cell, 39:209-221, 2010

PubMed Abstract: We report an interaction between poxA, encoding a paralog of lysyl tRNA-synthetase, and the closely linked yjeK gene, encoding a putative 2,3-beta-lysine aminomutase, that is critical for virulence and stress resistance in Salmonella enterica. Salmonella poxA and yjeK mutants share extensive phenotypic pleiotropy, including attenuated virulence in mice, an increased ability to respire under nutrient-limiting conditions, hypersusceptibility to a variety of diverse growth inhibitors, and altered expression of multiple proteins, including several encoded on the SPI-1 pathogenicity island. PoxA mediates posttranslational modification of bacterial elongation factor P (EF-P), analogous to the modification of the eukaryotic EF-P homolog, eIF5A, with hypusine. The modification of EF-P is a mechanism of regulation whereby PoxA acts as an aminoacyl-tRNA synthetase that attaches an amino acid to a protein resembling tRNA rather than to a tRNA.

PubMed: 20670890
DOI: 10.1016/j.molcel.2010.06.021

Experimental method

X-RAY DIFFRACTION (1.95 Å)