1ZLK

Crystal Structure of the Mycobacterium tuberculosis Hypoxic Response Regulator DosR C-terminal Domain-DNA Complex

Summary for 1ZLK

• Entry DOI: 10.2210/pdb1zlk/pdb
• Related: 1ZLJ
• Descriptor: 5'-D(*GP*GP*CP*CP*CP*GP*CP*GP*CP*TP*TP*TP*GP*GP*GP*GP*AP*CP*TP*AP*AP*AP*GP*TP*CP*CP*CP*TP*AP*AP*CP*CP*CP*TP*GP*GP*CP*CP*AP*CP*GP*AP*T)-3', 5'-D(*CP*GP*TP*GP*GP*CP*CP*AP*GP*GP*GP*TP*TP*AP*GP*GP*GP*AP*CP*TP*TP*TP*AP*GP*TP*CP*CP*CP*CP*AP*AP*AP*GP*CP*GP*CP*GP*GP*GP*CP*CP*AP*T)-3', Dormancy Survival Regulator (3 entities in total)
• Functional Keywords: helix-turn-helix, protein-dna complex, transcription-dna complex, transcription/dna
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 4
• Total formula weight: 47512.94

Authors

Wisedchaisri, G.,Wu, M.,Rice, A.E.,Roberts, D.M.,Sherman, D.R.,Hol, W.G.J. (deposition date: 2005-05-06, release date: 2006-01-31, Last modification date: 2023-08-23)

Primary citation

Wisedchaisri, G.,Wu, M.,Rice, A.E.,Roberts, D.M.,Sherman, D.R.,Hol, W.G.J.
Structures of Mycobacterium tuberculosis DosR and DosR-DNA complex involved in gene activation during adaptation to hypoxic latency.
J.Mol.Biol., 354:630-641, 2005

PubMed Abstract: On encountering low oxygen conditions, DosR activates the transcription of 47 genes, promoting long-term survival of Mycobacterium tuberculosis in a non-replicating state. Here, we report the crystal structures of the DosR C-terminal domain and its complex with a consensus DNA sequence of the hypoxia-induced gene promoter. The DosR C-terminal domain contains four alpha-helices and forms tetramers consisting of two dimers with non-intersecting dyads. In the DNA-bound structure, each DosR C-terminal domain in a dimer places its DNA-binding helix deep into the major groove, causing two bends in the DNA. DosR makes numerous protein-DNA base contacts using only three amino acid residues per subunit: Lys179, Lys182, and Asn183. The DosR tetramer is unique among response regulators with known structures.

PubMed: 16246368
DOI: 10.1016/j.jmb.2005.09.048

Experimental method

X-RAY DIFFRACTION (3.1 Å)