Publisher： John Wiley & Sons Inc
E-ISSN： 1744-3091|65|8|770-772
ISSN： 1744-3091
Source： Acta Crystallographica Section F, Vol.65, Iss.8, 2009-08, pp. : 770-772
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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 P3x21 and diffracted to 2.7 Å resolution. Crystal form I of Cps4B belonged to space‐group family P4x212 and diffracted to 2.8 Å resolution; crystal form II belonged to space group P212121 and diffracted to 1.9 Å resolution.
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