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Structural and Functional Aspects of the Sensor Histidine Kinase PrrB from Mycobacterium tuberculosis

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Structural and Functional Aspects of the Sensor Histidine Kinase PrrB from Mycobacterium tuberculosis. / Nowak, E.; Panjikar, S.; Morth, J.P.; Jordanova, R.; Svergun, D.I.; Tucker, P.A.

I: Structure, Bind 14, Nr. 2, 2006, s. 275-285.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Nowak, E, Panjikar, S, Morth, JP, Jordanova, R, Svergun, DI & Tucker, PA 2006, 'Structural and Functional Aspects of the Sensor Histidine Kinase PrrB from Mycobacterium tuberculosis', Structure, bind 14, nr. 2, s. 275-285.

APA

Nowak, E., Panjikar, S., Morth, J. P., Jordanova, R., Svergun, D. I., & Tucker, P. A. (2006). Structural and Functional Aspects of the Sensor Histidine Kinase PrrB from Mycobacterium tuberculosis. Structure, 14(2), 275-285.

CBE

Nowak E, Panjikar S, Morth JP, Jordanova R, Svergun DI, Tucker PA. 2006. Structural and Functional Aspects of the Sensor Histidine Kinase PrrB from Mycobacterium tuberculosis. Structure. 14(2):275-285.

MLA

Vancouver

Nowak E, Panjikar S, Morth JP, Jordanova R, Svergun DI, Tucker PA. Structural and Functional Aspects of the Sensor Histidine Kinase PrrB from Mycobacterium tuberculosis. Structure. 2006;14(2):275-285.

Author

Nowak, E. ; Panjikar, S. ; Morth, J.P. ; Jordanova, R. ; Svergun, D.I. ; Tucker, P.A. / Structural and Functional Aspects of the Sensor Histidine Kinase PrrB from Mycobacterium tuberculosis. I: Structure. 2006 ; Bind 14, Nr. 2. s. 275-285.

Bibtex

@article{709ae6600a7611dbbee902004c4f4f50,
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 three-domain 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.",
author = "E. Nowak and S. Panjikar and J.P. Morth and R. Jordanova and D.I. Svergun and P.A. Tucker",
year = "2006",
language = "English",
volume = "14",
pages = "275--285",
journal = "Structure",
issn = "0969-2126",
publisher = "Cell Press",
number = "2",

}

RIS

TY - JOUR

T1 - Structural and Functional Aspects of the Sensor Histidine Kinase PrrB from Mycobacterium tuberculosis

AU - Nowak, E.

AU - Panjikar, S.

AU - Morth, J.P.

AU - Jordanova, R.

AU - Svergun, D.I.

AU - Tucker, P.A.

PY - 2006

Y1 - 2006

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 three-domain 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 three-domain 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.

M3 - Journal article

VL - 14

SP - 275

EP - 285

JO - Structure

JF - Structure

SN - 0969-2126

IS - 2

ER -