Summary information and primary citation

PDB-id
1zlk; DSSR-derived features in text and JSON formats
Class
transcription-DNA
Method
X-ray (3.1 Å)
Summary
Crystal structure of the mycobacterium tuberculosis hypoxic response regulator dosr c-terminal domain-DNA complex
Reference
Wisedchaisri G, Wu M, Rice AE, Roberts DM, Sherman DR, Hol WGJ (2005): "Structures of Mycobacterium tuberculosis DosR and DosR-DNA complex involved in gene activation during adaptation to hypoxic latency." J.Mol.Biol., 354, 630-641. doi: 10.1016/j.jmb.2005.09.048.
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.

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