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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...
Autores principales: | , , , |
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Formato: | Texto |
Lenguaje: | English |
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International Union of Crystallography
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2720329/ https://www.ncbi.nlm.nih.gov/pubmed/19652335 http://dx.doi.org/10.1107/S1744309109023914 |
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author | Huang, Hexian Hagelueken, Gregor Whitfield, Chris Naismith, James H. |
author_facet | Huang, Hexian Hagelueken, Gregor Whitfield, Chris Naismith, James H. |
author_sort | Huang, Hexian |
collection | PubMed |
description | 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 Å resolution. Crystal form I of Cps4B belonged to space-group family P4(x)2(1)2 and diffracted to 2.8 Å resolution; crystal form II belonged to space group P2(1)2(1)2(1) and diffracted to 1.9 Å resolution. |
format | Text |
id | pubmed-2720329 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-27203292009-08-13 Crystallization and preliminary crystallographic analysis of the bacterial capsule assembly-regulating tyrosine phosphatases Wzb of Escherichia coli and Cps4B of Streptococcus pneumoniae Huang, Hexian Hagelueken, Gregor Whitfield, Chris Naismith, James H. Acta Crystallogr Sect F Struct Biol Cryst Commun Crystallization Communications 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 Å resolution. Crystal form I of Cps4B belonged to space-group family P4(x)2(1)2 and diffracted to 2.8 Å resolution; crystal form II belonged to space group P2(1)2(1)2(1) and diffracted to 1.9 Å resolution. International Union of Crystallography 2009-07-25 /pmc/articles/PMC2720329/ /pubmed/19652335 http://dx.doi.org/10.1107/S1744309109023914 Text en © Huang et al. 2009 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
spellingShingle | Crystallization Communications Huang, Hexian Hagelueken, Gregor Whitfield, Chris Naismith, James H. Crystallization and preliminary crystallographic analysis of the bacterial capsule assembly-regulating tyrosine phosphatases Wzb of Escherichia coli and Cps4B of Streptococcus pneumoniae |
title | Crystallization and preliminary crystallographic analysis of the bacterial capsule assembly-regulating tyrosine phosphatases Wzb of Escherichia coli and Cps4B of Streptococcus pneumoniae
|
title_full | Crystallization and preliminary crystallographic analysis of the bacterial capsule assembly-regulating tyrosine phosphatases Wzb of Escherichia coli and Cps4B of Streptococcus pneumoniae
|
title_fullStr | Crystallization and preliminary crystallographic analysis of the bacterial capsule assembly-regulating tyrosine phosphatases Wzb of Escherichia coli and Cps4B of Streptococcus pneumoniae
|
title_full_unstemmed | Crystallization and preliminary crystallographic analysis of the bacterial capsule assembly-regulating tyrosine phosphatases Wzb of Escherichia coli and Cps4B of Streptococcus pneumoniae
|
title_short | Crystallization and preliminary crystallographic analysis of the bacterial capsule assembly-regulating tyrosine phosphatases Wzb of Escherichia coli and Cps4B of Streptococcus pneumoniae
|
title_sort | crystallization and preliminary crystallographic analysis of the bacterial capsule assembly-regulating tyrosine phosphatases wzb of escherichia coli and cps4b of streptococcus pneumoniae |
topic | Crystallization Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2720329/ https://www.ncbi.nlm.nih.gov/pubmed/19652335 http://dx.doi.org/10.1107/S1744309109023914 |
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