Role of a PAS sensor domain in the Mycobacterium tuberculosis transcription regulator Rv1364c


Autoria(s): Jaiswal, Ravi Kumar; Manjeera, G; Gopal, B
Data(s)

30/07/2010

Resumo

The Mycobacterium tuberculosis transcriptional regulator Rv1364c regulates the activity of the stress response sigma factor sigma(F). This multi-domain protein has several components: a signaling PAS domain and an effector segment comprising of a phosphatase, a kinase and an anti-anti-sigma factor domain. Based on Small Angle X-ray Scattering (SAXS) data, Rv1364c was recently shown to be a homo-dimer and adopt an elongated conformation in solution. The PAS domain could not be modeled into the structural envelope due to poor sequence similarity with known PAS proteins. The crystal structure of the PAS domain described here provides a structural basis for the dimerization of Rv1364c. It thus appears likely that the PAS domain regulates the anti-sigma activity of Rv1364c by oligomerization. A structural comparison with other characterized PAS domains reveal several sequence and conformational features that could facilitate ligand binding - a feature which suggests that the function of Rv1364c could potentially be governed by specific cellular signals or metabolic cues. (C) 2010 Elsevier Inc. All rights reserved.

Formato

application/pdf

Identificador

http://eprints.iisc.ernet.in/32001/1/pas.pdf

Jaiswal, Ravi Kumar and Manjeera, G and Gopal, B (2010) Role of a PAS sensor domain in the Mycobacterium tuberculosis transcription regulator Rv1364c. In: Biochemical and Biophysical Research Communications, 398 (3). pp. 342-349.

Publicador

Elsevier Science

Relação

http://dx.doi.org/10.1016/j.bbrc.2010.06.027

http://eprints.iisc.ernet.in/32001/

Palavras-Chave #Molecular Biophysics Unit
Tipo

Journal Article

PeerReviewed