2fez

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|ACTIVITY=
|ACTIVITY=
|GENE= embR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])
|GENE= embR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fez OCA], [http://www.ebi.ac.uk/pdbsum/2fez PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fez RCSB]</span>
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}}
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[[Category: Besra, G S.]]
[[Category: Besra, G S.]]
[[Category: Futterer, K.]]
[[Category: Futterer, K.]]
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[[Category: transcriptional regulator; winged-helix; tetratricopeptide repeat; beta-sandwich;]]
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[[Category: beta-sandwich;]]
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[[Category: tetratricopeptide repeat]]
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[[Category: transcriptional regulator]]
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[[Category: winged-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:01:56 2008''

Revision as of 00:01, 31 March 2008


PDB ID 2fez

Drag the structure with the mouse to rotate
, resolution 2.00Å
Gene: embR (Mycobacterium tuberculosis)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Mycobacterium tuberculosis EmbR


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

2FEZ is a Single protein structure of sequence 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

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