2ff4: Difference between revisions
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|PDB= 2ff4 |SIZE=350|CAPTION= <scene name='initialview01'>2ff4</scene>, resolution 1.90Å | |PDB= 2ff4 |SIZE=350|CAPTION= <scene name='initialview01'>2ff4</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene> | ||
|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]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[2fez|2FEZ]] | |||
|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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[[Category: Besra, G S.]] | [[Category: Besra, G S.]] | ||
[[Category: Futterer, K.]] | [[Category: Futterer, K.]] | ||
[[Category: | [[Category: beta-sandwich]] | ||
[[Category: tetratricopeptide repeat]] | |||
[[Category: winged-helix]] | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:02:02 2008'' | ||
Revision as of 03:02, 31 March 2008
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| , resolution 1.90Å | |||||||
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| Ligands: | |||||||
| Gene: | embR (Mycobacterium tuberculosis) | ||||||
| Related: | 2FEZ
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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