3KX0

Crystal Structure of the PAS domain of Rv1364c

Summary for 3KX0

• Entry DOI: 10.2210/pdb3kx0/pdb
• Related: 3fc7 3fg8
• Descriptor: Uncharacterized protein Rv1364c/MT1410, ISOPROPYL ALCOHOL (3 entities in total)
• Functional Keywords: pas domain, rv1364c, sensory domain, mycobacteium tuberculosis, small molecule binding domain, signaling protein
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 21169.60

Authors

Jaiswal, R.K.,Gopal, B. (deposition date: 2009-12-02, release date: 2010-06-23, Last modification date: 2024-11-13)

Primary citation

Jaiswal, R.K.,Manjeera, G.,Gopal, B.
Role of a PAS sensor domain in the Mycobacterium tuberculosis transcription regulator Rv1364c
Biochem.Biophys.Res.Commun., 398:342-349, 2010

PubMed Abstract: 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.

PubMed: 20541534
DOI: 10.1016/j.bbrc.2010.06.027

Experimental method

X-RAY DIFFRACTION (2.3 Å)