Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:1.95
Classification:LIGASE
Release Date:2009-03-10
Deposition Date:2009-01-30
Revision Date:2011-07-13#2011-10-12
Molecular Weight:75209.27
Macromolecule Type:Protein
Residue Count:652
Atom Site Count:5305
DOI:10.2210/pdb3g1z/pdb
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.
Resolution:1.95
Classification:LIGASE
Release Date:2009-03-10
Deposition Date:2009-01-30
Revision Date:2011-07-13#2011-10-12
Molecular Weight:75209.27
Macromolecule Type:Protein
Residue Count:652
Atom Site Count:5305
DOI:10.2210/pdb3g1z/pdb
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.
| Date made available | 2009 |
|---|---|
| Publisher | RCSB-PDB |