2FEZ

Mycobacterium tuberculosis EmbR

Summary for 2FEZ

• Entry DOI: 10.2210/pdb2fez/pdb
• Descriptor: Probable regulatory protein embR (2 entities in total)
• Functional Keywords: transcriptional regulator; winged-helix; tetratricopeptide repeat; beta-sandwich;, transcription
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 41988.38

Authors

Futterer, K.,Alderwick, L.J.,Besra, G.S. (deposition date: 2005-12-17, release date: 2006-01-24, Last modification date: 2024-02-14)

Primary citation

Alderwick, L.J.,Molle, V.,Kremer, L.,Cozzone, A.J.,Dafforn, T.R.,Besra, G.S.,Futterer, K.
Molecular structure of EmbR, a response element of Ser/Thr kinase signaling in Mycobacterium tuberculosis
Proc.Natl.Acad.Sci.Usa, 103:2558-2563, 2006

PubMed 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.

PubMed: 16477027
DOI: 10.1073/pnas.0507766103

Experimental method

X-RAY DIFFRACTION (2 Å)