2fez
From Proteopedia
(New page: 200px<br /><applet load="2fez" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fez, resolution 2.00Å" /> '''Mycobacterium tuberc...) |
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| - | [[Image:2fez.gif|left|200px]]<br /><applet load="2fez" size=" | + | [[Image:2fez.gif|left|200px]]<br /><applet load="2fez" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2fez, resolution 2.00Å" /> | caption="2fez, resolution 2.00Å" /> | ||
'''Mycobacterium tuberculosis EmbR'''<br /> | '''Mycobacterium tuberculosis EmbR'''<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== | ||
| - | 2FEZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http:// | + | 2FEZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=2FEZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Alderwick, L | + | [[Category: Alderwick, L J.]] |
| - | [[Category: Besra, G | + | [[Category: Besra, G S.]] |
[[Category: Futterer, K.]] | [[Category: Futterer, K.]] | ||
[[Category: transcriptional regulator; winged-helix; tetratricopeptide repeat; beta-sandwich;]] | [[Category: transcriptional regulator; winged-helix; tetratricopeptide repeat; beta-sandwich;]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:47 2008'' |
Revision as of 15:20, 21 February 2008
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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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