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2ff4

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[[Image:2ff4.gif|left|200px]]
[[Image:2ff4.gif|left|200px]]
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{{Structure
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|GENE= embR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])
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{{STRUCTURE_2ff4| PDB=2ff4 | SCENE= }}
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|RELATEDENTRY=[[2fez|2FEZ]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ff4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ff4 OCA], [http://www.ebi.ac.uk/pdbsum/2ff4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ff4 RCSB]</span>
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'''Mycobacterium tuberculosis EmbR in complex with low affinity phosphopeptide'''
'''Mycobacterium tuberculosis EmbR in complex with low affinity phosphopeptide'''
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[[Category: Besra, G S.]]
[[Category: Besra, G S.]]
[[Category: Futterer, K.]]
[[Category: Futterer, K.]]
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[[Category: beta-sandwich]]
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[[Category: Beta-sandwich]]
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[[Category: tetratricopeptide repeat]]
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[[Category: Tetratricopeptide repeat]]
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[[Category: winged-helix]]
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[[Category: Winged-helix]]
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Revision as of 00:49, 4 May 2008

Template:STRUCTURE 2ff4

Mycobacterium tuberculosis EmbR in complex with low affinity phosphopeptide


Overview

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 Structure

2FF4 is a Protein complex structure of sequences from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sun May 4 03:49:22 2008

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