2ff4: Difference between revisions
New page: left|200px<br /><applet load="2ff4" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ff4, resolution 1.90Å" /> '''Mycobacterium tuberc... |
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[[Image:2ff4.gif|left|200px]]<br /><applet load="2ff4" size=" | [[Image:2ff4.gif|left|200px]]<br /><applet load="2ff4" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2ff4, resolution 1.90Å" /> | caption="2ff4, resolution 1.90Å" /> | ||
'''Mycobacterium tuberculosis EmbR in complex with low affinity phosphopeptide'''<br /> | '''Mycobacterium tuberculosis EmbR in complex with low affinity phosphopeptide'''<br /> | ||
==Overview== | ==Overview== | ||
Ser/Thr phosphorylation has emerged as a critical regulatory mechanism in | 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== | ==About this Structure== | ||
2FF4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http:// | 2FF4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FF4 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Alderwick, L | [[Category: Alderwick, L J.]] | ||
[[Category: Besra, G | [[Category: Besra, G S.]] | ||
[[Category: Futterer, K.]] | [[Category: Futterer, K.]] | ||
[[Category: winged-helix; tetratricopeptide repeat; beta-sandwich]] | [[Category: winged-helix; tetratricopeptide repeat; beta-sandwich]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:45 2008'' | ||
Revision as of 15:20, 21 February 2008
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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
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