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

Hexian Huang, Gregor Hagelueken, Chris Whitfield, James H. Naismith

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

Abstract

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 in Gram-positive bacteria such as Streptococcus pneumoniae (CpsCD and CpsB). Although Wzb and Cps4B are both predicted to dephosphorylate the C-terminal tyrosine cluster of their cognate tyrosine kinase, they appear on the basis of protein sequence to belong to quite different enzyme classes. Recombinant purified proteins Cps4B of S. pneumoniae TIGR4 and Wzb of E. coli K-30 have been crystallized. Wzb crystals belonged to space-group family P3(x)21 and diffracted to 2.7 angstrom resolution. Crystal form I of Cps4B belonged to space-group family P4(x)2(1)2 and diffracted to 2.8 angstrom resolution; crystal form II belonged to space group P2(1)2(1)2(1) and diffracted to 1.9 angstrom resolution.

Original languageEnglish
Pages (from-to)770-772
Number of pages3
JournalActa Crystallographica. Section F, Structural biology and crystallization communications
Volume65
DOIs
Publication statusPublished - Aug 2009

Keywords

  • POLYSACCHARIDES
  • PHOSPHORYLATION
  • BIOSYNTHESIS

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