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

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...

Full description

Saved in:
Bibliographic Details
Published inActa 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
LanguageEnglish
Published 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.08.2009
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary: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.
Bibliography:ArticleID:AYF2NJ5040
istex:1FB577CE7E288D3E226A57118CFF625ACC853134
ark:/67375/WNG-5NHFXNQL-G
ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ObjectType-Article-1
ObjectType-Feature-2
These authors contributed equally.
ISSN:1744-3091
1744-3091
DOI:10.1107/S1744309109023914