PDBsum entry 3kx0

Signaling protein

PDB id: 3kx0

Contents

Protein chain

127 a.a. *

Ligands

IPA

Waters ×5

* Residue conservation analysis

PDB id:

3kx0

Name:

Signaling protein

Title:

Crystal structure of the pas domain of rv1364c

Structure:

Uncharacterized protein rv1364c/mt1410. Chain: x. Fragment: unp residues 1-163. Engineered: yes

Source:

Mycobacterium tuberculosis. Organism_taxid: 1773. Strain: h37rv. Gene: rv1364c. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.30Å R-factor: 0.235 R-free: 0.274

Authors:

R.K.Jaiswal,B.Gopal

Key ref:

R.K.Jaiswal et al. (2010). Role of a PAS sensor domain in the Mycobacterium tuberculosis transcription regulator Rv1364c. Biochem Biophys Res Commun, 398, 342-349. PubMed id: 20541534

Date:

02-Dec-09 Release date: 23-Jun-10

Protein chain

P9WLZ7  (Y1364_MYCTU) -  Multidomain regulatory protein Rv1364c from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

Seq: 653 a.a.

Struc: 127 a.a.

Enzyme reactions

• Enzyme class 2: E.C.2.7.11.1 - non-specific serine/threonine protein kinase.
• Reaction:
  1. L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H⁺
  2. L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H⁺
• Enzyme class 3: E.C.3.1.3.16 - protein-serine/threonine phosphatase.
• Reaction:
  1. O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] + phosphate
  2. O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] + phosphate

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

Biochem Biophys Res Commun 398:342-349 (2010)

PubMed id: 20541534

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

R.K.Jaiswal, G.Manjeera, B.Gopal.

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.