Structural and functional aspects of the sensor histidine kinase PrrB from Mycobacterium tuberculosis

E Nowak; S Panjikar; JP Morth; R Jordanova; DI Svergun; PA Tucker

doi:10.1016/j.str.2005.10.006

Structural and functional aspects of the sensor histidine kinase PrrB from Mycobacterium tuberculosis

E Nowak, S Panjikar, JP Morth, R Jordanova, DI Svergun, PA Tucker^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

39 Citations (Scopus)

Abstract

We describe the solution structures of two- and three-domain constructs of the sensor histidine kinase PrrB from Mycobacterium tuberculosis, which allow us to locate the HAMP linker relative to the ATP binding and dimerization domains. We show that the threedomain construct is active both for autophosphorylation and for phosphotransfer to the cognate response regulator, PrrA. We also describe the high-resolution crystal structure of the catalytic domain alone, and we show that, in solution, it binds ATP. The conformational flexibility of this domain is discussed and related to other structural information.

Original language	English
Pages (from-to)	275-285
Number of pages	11
Journal	Structure
Volume	14
Issue number	2
DOIs	https://doi.org/10.1016/j.str.2005.10.006
Publication status	Published - Feb-2006
Externally published	Yes

Keywords

RAY SOLUTION SCATTERING
ELECTRON-DENSITY MAPS
2-COMPONENT SYSTEM
BIOLOGICAL MACROMOLECULES
CRYSTAL-STRUCTURE
ESCHERICHIA-COLI
GENE-EXPRESSION
PROTEIN MODELS
DOMAIN
DIFFRACTION

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title = "Structural and functional aspects of the sensor histidine kinase PrrB from Mycobacterium tuberculosis",

abstract = "We describe the solution structures of two- and three-domain constructs of the sensor histidine kinase PrrB from Mycobacterium tuberculosis, which allow us to locate the HAMP linker relative to the ATP binding and dimerization domains. We show that the threedomain construct is active both for autophosphorylation and for phosphotransfer to the cognate response regulator, PrrA. We also describe the high-resolution crystal structure of the catalytic domain alone, and we show that, in solution, it binds ATP. The conformational flexibility of this domain is discussed and related to other structural information.",

keywords = "RAY SOLUTION SCATTERING, ELECTRON-DENSITY MAPS, 2-COMPONENT SYSTEM, BIOLOGICAL MACROMOLECULES, CRYSTAL-STRUCTURE, ESCHERICHIA-COLI, GENE-EXPRESSION, PROTEIN MODELS, DOMAIN, DIFFRACTION",

author = "E Nowak and S Panjikar and JP Morth and R Jordanova and DI Svergun and PA Tucker",

year = "2006",

month = feb,

doi = "10.1016/j.str.2005.10.006",

language = "English",

volume = "14",

pages = "275--285",

journal = "Structure",

issn = "0969-2126",

publisher = "Cell Press",

number = "2",

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TY - JOUR

T1 - Structural and functional aspects of the sensor histidine kinase PrrB from Mycobacterium tuberculosis

AU - Nowak, E

AU - Panjikar, S

AU - Morth, JP

AU - Jordanova, R

AU - Svergun, DI

AU - Tucker, PA

PY - 2006/2

Y1 - 2006/2

N2 - We describe the solution structures of two- and three-domain constructs of the sensor histidine kinase PrrB from Mycobacterium tuberculosis, which allow us to locate the HAMP linker relative to the ATP binding and dimerization domains. We show that the threedomain construct is active both for autophosphorylation and for phosphotransfer to the cognate response regulator, PrrA. We also describe the high-resolution crystal structure of the catalytic domain alone, and we show that, in solution, it binds ATP. The conformational flexibility of this domain is discussed and related to other structural information.

AB - We describe the solution structures of two- and three-domain constructs of the sensor histidine kinase PrrB from Mycobacterium tuberculosis, which allow us to locate the HAMP linker relative to the ATP binding and dimerization domains. We show that the threedomain construct is active both for autophosphorylation and for phosphotransfer to the cognate response regulator, PrrA. We also describe the high-resolution crystal structure of the catalytic domain alone, and we show that, in solution, it binds ATP. The conformational flexibility of this domain is discussed and related to other structural information.

KW - RAY SOLUTION SCATTERING

KW - ELECTRON-DENSITY MAPS

KW - 2-COMPONENT SYSTEM

KW - BIOLOGICAL MACROMOLECULES

KW - CRYSTAL-STRUCTURE

KW - ESCHERICHIA-COLI

KW - GENE-EXPRESSION

KW - PROTEIN MODELS

KW - DOMAIN

KW - DIFFRACTION

U2 - 10.1016/j.str.2005.10.006

DO - 10.1016/j.str.2005.10.006

M3 - Article

SN - 0969-2126

VL - 14

SP - 275

EP - 285

JO - Structure

JF - Structure

IS - 2

ER -

Structural and functional aspects of the sensor histidine kinase PrrB from Mycobacterium tuberculosis

Abstract

Keywords

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