PMID:16477027

Citation	Alderwick, LJ, Molle, V, Kremer, L, Cozzone, AJ, Dafforn, TR, Besra, GS and Fütterer, K (2006) Molecular structure of EmbR, a response element of Ser/Thr kinase signaling in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U.S.A. 103:2558-63
Abstract	Ser/Thr phosphorylation has emerged as a critical regulatory mechanism in a number of bacteria, including Mycobacterium tuberculosis. This problematic pathogen encodes 11 eukaryotic-like Ser/Thr kinases, yet few substrates or signaling targets have been characterized. Here, we report the structure of EmbR (2.0 A), a putative transcriptional regulator of key arabinosyltransferases (EmbC, -A, and -B), and an endogenous substrate of the Ser/Thr-kinase PknH. EmbR presents a unique domain architecture: the N-terminal winged-helix DNA-binding domain forms an extensive interface with the all-helical central bacterial transcriptional activation domain and is positioned adjacent to the regulatory C-terminal forkhead-associated (FHA) domain, which mediates binding to a Thr-phosphorylated site in PknH. The structure in complex with a phospho-peptide (1.9 A) reveals a conserved mode of phospho-threonine recognition by the FHA domain and evidence for specific recognition of the cognate kinase. The present structures suggest hypotheses as to how EmbR might propagate the phospho-relay signal from its cognate kinase, while serving as a template for the structurally uncharacterized Streptomyces antibiotic regulatory protein family of transcription factors.
Links	PubMed PMC1413777 Online version:10.1073/pnas.0507766103
Keywords	Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/metabolism; Gene Expression Regulation, Bacterial; Mycobacterium tuberculosis/enzymology; Mycobacterium tuberculosis/genetics; Mycobacterium tuberculosis/metabolism; Peptides/chemistry; Phosphorylation; Protein Structure, Tertiary; Protein-Serine-Threonine Kinases/genetics; Response Elements; Transcription Factors/chemistry; Transcription Factors/metabolism; X-Ray Diffraction
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