Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3QYX

Crystal structure of Mycobacterium tuberculosis EspR in complex with a small DNA fragment

Summary for 3QYX
Entry DOI10.2210/pdb3qyx/pdb
Related3QF3 3QWG
DescriptorESX-1 secretion-associated regulator EspR, 5'-D(*A*CP*GP*CP*CP*GP*AP*AP*TP*C)-3' (2 entities in total)
Functional Keywordsn-terminal hth motif, c-terminal dimerization domain, dna-binding, transcription factor, dimer of dimers binding dna, transcription activator, transcription-dna complex, transcription/dna
Biological sourceMycobacterium tuberculosis
Cellular locationSecreted: P96228
Total number of polymer chains5
Total formula weight61980.38
Authors
Blasco, B.,Pojer, F.,Cole, S.T. (deposition date: 2011-03-04, release date: 2011-09-14, Last modification date: 2024-04-03)
Primary citationBlasco, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.75 Å)
Structure validation

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon