1ZYL

Crystal Structure of Hypothetical Protein YihE from Escherichia coli

Summary for 1ZYL

• Entry DOI: 10.2210/pdb1zyl/pdb
• Descriptor: Hypothetical protein yihE (1 entity in total)
• Functional Keywords: hypothetical protein, putative protein kinase, structural genomics, psi, protein structure initiative, montreal-kingston bacterial structural genomics initiative, bsgi, unknown function
• Biological source: Escherichia coli
• Cellular location: Cytoplasm (By similarity): P0C0K3
• Total number of polymer chains: 1
• Total formula weight: 38160.18

Authors

Zheng, J.,Jia, Z.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2005-06-10, release date: 2006-09-19, Last modification date: 2024-02-14)

Primary citation

Zheng, J.,He, C.,Singh, V.K.,Martin, N.L.,Jia, Z.
Crystal structure of a novel prokaryotic Ser/Thr kinase and its implication in the Cpx stress response pathway.
Mol.Microbiol., 63:1360-1371, 2007

PubMed Abstract: The Cpx signalling system of Escherichia coli and Salmonella enterica senses extracytoplasmic stress and controls expression of factors that allow the bacterium to adapt to these stressors and thereby enhance survival. Many of the Cpx-responsive genes products are of unknown function. We determined the crystal structure of one of these gene products, called YihE in E. coli, which exhibits a eukaryotic kinase fold. Functional assays established that both YihE and the S. enterica YihE homologue, RdoA, undergo autophosphorylation and phosphorylate protein substrates at Ser/Thr residues in vitro, demonstrating that YihE/RdoA is a novel Ser/Thr protein kinase in prokaryotic cells. Phenotypic analysis of yihE/rdoA null strains indicates that this kinase is most abundant in stationary phase, and is important for long-term cell survival and for expression of surface appendages in both a Cpx-independent and -dependent manner. YihE/RdoA is therefore a previously unknown kinase component of a new type of bacterial phosphorelay mechanism, adding kinase activity as another response to the Cpx sensing system that functions to maintain cellular homeostasis.

PubMed: 17302814
DOI: 10.1111/j.1365-2958.2007.05611.x

Experimental method

X-RAY DIFFRACTION (2.8 Å)