2ff4
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Mycobacterium tuberculosis EmbR in complex with low affinity phosphopeptide
OverviewOverview
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.
About this StructureAbout this Structure
2FF4 is a Protein complex structure of sequences from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
ReferenceReference
Molecular structure of EmbR, a response element of Ser/Thr kinase signaling in Mycobacterium tuberculosis., Alderwick LJ, Molle V, Kremer L, Cozzone AJ, Dafforn TR, Besra GS, Futterer K, Proc Natl Acad Sci U S A. 2006 Feb 21;103(8):2558-63. Epub 2006 Feb 13. PMID:16477027
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