Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
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.
Structures of Mycobacterium tuberculosis DosR and DosR-DNA complex involved in gene activation during adaptation to hypoxic latency.,Wisedchaisri G, Wu M, Rice AE, Roberts DM, Sherman DR, Hol WG J Mol Biol. 2005 Dec 2;354(3):630-41. Epub 2005 Oct 3. PMID:16246368[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wisedchaisri G, Wu M, Rice AE, Roberts DM, Sherman DR, Hol WG. Structures of Mycobacterium tuberculosis DosR and DosR-DNA complex involved in gene activation during adaptation to hypoxic latency. J Mol Biol. 2005 Dec 2;354(3):630-41. Epub 2005 Oct 3. PMID:16246368 doi:10.1016/j.jmb.2005.09.048
