3QWG
Crystal structure of EspRdelta10, C-terminal 10 amino acids deletion mutant of EspR transcription factor from Mycobacterium tuberculosis
Summary for 3QWG
| Entry DOI | 10.2210/pdb3qwg/pdb |
| Related | 3QF3 3QYX |
| Descriptor | ESX-1 secretion-associated regulator EspR (2 entities in total) |
| Functional Keywords | n-terminal helix-turn-helix motif, transcription factor, transcription |
| Biological source | Mycobacterium tuberculosis |
| Cellular location | Secreted: P96228 |
| Total number of polymer chains | 2 |
| Total formula weight | 27256.74 |
| Authors | Blasco, B.,Pojer, F.,Cole, S.T. (deposition date: 2011-02-28, release date: 2011-09-14, Last modification date: 2023-09-13) |
| 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 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: 21883526DOI: 10.1111/j.1365-2958.2011.07813.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.992 Å) |
Structure validation
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