3QF3

Crystal structure of EspR transcription factor from mycobacterium tuberculosis

Summary for 3QF3

• Entry DOI: 10.2210/pdb3qf3/pdb
• Related: 3QWG 3QYX
• Descriptor: ESX-1 secretion-associated regulator EspR, (2S)-2-hydroxybutanedioic acid, D-MALATE, ... (4 entities in total)
• Functional Keywords: n-terminal hth motif, c-terminal dimerization domain, transcription factor, homodimer, transcription
• Biological source: Mycobacterium tuberculosis
• Cellular location: Secreted: P96228
• Total number of polymer chains: 6
• Total formula weight: 88851.84

Authors

Blasco, B.,Pojer, F.,Cole, S.T. (deposition date: 2011-01-21, release date: 2011-09-14, Last modification date: 2024-04-03)

Primary citation

Blasco, B.,Stenta, M.,Alonso-Sarduy, L.,Dietler, G.,Peraro, M.D.,Cole, S.T.,Pojer, F.
Atypical DNA recognition mechanism used by the EspR virulence regulator of Mycobacterium tuberculosis.
Mol.Microbiol., 82:251-264, 2011

PubMed Abstract: The human pathogen Mycobacterium tuberculosis requires the ESX-1 secretion system for full virulence. EspR plays a key role in ESX-1 regulation via direct binding and transcriptional activation of the espACD operon. Here, we describe the crystal structures of EspR, a C-terminally truncated form, EspRΔ10, as well as an EspR-DNA complex. EspR forms a dimer with each monomer containing an N-terminal helix-turn-helix DNA binding motif and an atypical C-terminal dimerization domain. Structural studies combined with footprinting experiments, atomic force microscopy and molecular dynamic simulations allow us to propose a model in which a dimer of EspR dimers is the minimal functional unit with two subunits binding two consecutive major grooves. The other two DNA binding domains are thus free to form higher-order oligomers and to bridge distant DNA sites in a cooperative way. These features are reminiscent of nucleoid-associated proteins and suggest a more general regulatory role for EspR than was previously suspected.

PubMed: 21883526
DOI: 10.1111/j.1365-2958.2011.07813.x

Experimental method

X-RAY DIFFRACTION (2.41 Å)