Crystallization and preliminary crystallographic analysis of the bacterial capsule assembly-regulating tyrosine phosphatases Wzb of Escherichia coli and Cps4B of Streptococcus pneumoniae

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 65; no. 8; pp. 770 - 772
• Main Authors: Huang, Hexian, Hagelueken, Gregor, Whitfield, Chris, Naismith, James H.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.08.2009
• Subjects: Base Sequence; Cps4B; Crystallization; Crystallization Communications; Crystallography, X-Ray; DNA Primers; Escherichia coli; Escherichia coli - enzymology; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - genetics; kinases; phosphatases; Phosphoprotein Phosphatases - chemistry; Phosphoprotein Phosphatases - genetics; Polymerase Chain Reaction; Protein Tyrosine Phosphatases - chemistry; Protein Tyrosine Phosphatases - genetics; Recombinant Proteins - chemistry; Streptococcus; Streptococcus pneumoniae; Streptococcus pneumoniae - enzymology; Wzb

Bacterial tyrosine kinases and their cognate phosphatases are key players in the regulation of capsule assembly and thus are important virulence determinants of these bacteria. Examples of the kinase/phosphatase pairing are found in Gram‐negative bacteria such as Escherichia coli (Wzc and Wzb) and i...