Characterization of Salmonella typhimurium YegS, a putative lipid kinase homologous to eukaryotic sphingosine and diacylglycerol kinases.

Journal article

Salmonella typhimurium YegS is a protein conserved in many prokaryotes. Although the function of YegS is not definitively known, it has been annotated as a potential diacylglycerol or sphingosine kinase based on sequence similarity with eukaryotic enzymes of known function. To further characterize YegS, we report its purification, biochemical analysis, crystallization, and structure determination. The crystal structure of YegS reveals a two-domain fold related to bacterial polyphosphate/ATP N...

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Authors: Nichols, C; Lamb, H; Lockyer, M; Charles, I; Pyne, S

• Publication status: Published
• Journal: Proteins
• Volume: 68
• Issue: 1
• Pages: 13-25
• Publication date: 2007-07-01
• DOI: 10.1002/prot.21386
• EISSN: 1097-0134
• ISSN: 0887-3585
• Language: English
• Keywords: Binding Sites; Protein Structure, Tertiary; Models, Molecular; Calorimetry, Differential Scanning; Structural Homology, Protein; Protein Conformation; Salmonella typhimurium; Phosphotransferases (Alcohol Group Acceptor); Base Sequence; Amino Acid Sequence; Molecular Sequence Data; Crystallization; Protein Folding; Diacylglycerol Kinase; Mass Spectrometry; Bacterial Proteins; Sequence Analysis, DNA