Emerging structural insights into bacterial tyrosine kinases.
Bacterial protein tyrosine (Tyr) phosphorylation emerged as an exciting new field of research in the last decade. Of known bacterial Tyr (BY) kinases, most regulate the production of pathogenic capsular and extracellular polysaccharide in both Gram-positive and Gram-negative bacteria. The recent publications of the first two BY kinase structures, Etk from Escherichia coli and CapB from Staphylococcus aureus, reveal that the 3D folds bear no resemblance to their mammalian counterparts but instead are similar to those of the MinD ATPases from the P-loop NTPase superfamily. These structural studies provided the first glimpse into the functional machinery of BY kinases, including their enzymatic specificity and unique activation mechanisms, which are unlike anything observed in mammalian tyrosine kinases.
Lee
Daniel C
DC
Department of Biochemistry, Queen's University, Kingston, Ontario, Canada.
Jia
Zongchao
Z
D000251:Adenosine Triphosphatases / Q000737:chemistry; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D006090:Gram-Negative Bacteria / Q000201:enzymology*; D006094:Gram-Positive Bacteria / Q000201:enzymology*; D008969:Molecular Sequence Data; D010766:Phosphorylation; D017434:Protein Structure, Tertiary; D011505:Protein-Tyrosine Kinases / Q000737:chemistry* / Q000378:metabolism; D016415:Sequence Alignment; D013379:Substrate Specificity
D001426:Bacterial Proteins; D011505:Protein-Tyrosine Kinases; D000251:Adenosine Triphosphatases