1zlk
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(New page: 200px<br /><applet load="1zlk" size="350" color="white" frame="true" align="right" spinBox="true" caption="1zlk, resolution 3.10Å" /> '''Crystal Structure of...)
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Revision as of 15:37, 29 January 2008
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Crystal Structure of the Mycobacterium tuberculosis Hypoxic Response Regulator DosR C-terminal Domain-DNA Complex
Overview
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.
About this Structure
1ZLK is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
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
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