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...

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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
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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.
AbstractList 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 A resolution. Crystal form I of Cps4B belonged to space-group family P4(x)2(1)2 and diffracted to 2.8 A resolution; crystal form II belonged to space group P2(1)2(1)2(1) and diffracted to 1.9 A resolution.
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. pneumoniaeTIGR4 and Wzb of E. coliK-30 have been crystallized. Wzb crystals belonged to space-group family P3x21 and diffracted to 2.7 Aa resolution. Crystal form I of Cps4B belonged to space-group family P4x212 and diffracted to 2.8 Aa resolution; crystal form II belonged to space group P212121 and diffracted to 1.9 Aa resolution.
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.
The crystallization is reported of two bacterial tyrosine phosphatases which belong to different enzyme families despite their ability to catalyse identical reactions. 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 P 3 x 21 and diffracted to 2.7 Å resolution. Crystal form I of Cps4B belonged to space-group family P 4 x 2 1 2 and diffracted to 2.8 Å resolution; crystal form II belonged to space group P 2 1 2 1 2 1 and diffracted to 1.9 Å resolution.
Author Whitfield, Chris
Hagelueken, Gregor
Huang, Hexian
Naismith, James H.
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Snippet Bacterial tyrosine kinases and their cognate phosphatases are key players in the regulation of capsule assembly and thus are important virulence determinants...
The crystallization is reported of two bacterial tyrosine phosphatases which belong to different enzyme families despite their ability to catalyse identical...
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SubjectTerms 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
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Title Crystallization and preliminary crystallographic analysis of the bacterial capsule assembly-regulating tyrosine phosphatases Wzb of Escherichia coli and Cps4B of Streptococcus pneumoniae
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