This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2ff4
From Proteopedia
(New page: 200px<br /><applet load="2ff4" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ff4, resolution 1.90Å" /> '''Mycobacterium tuberc...) |
|||
| Line 1: | Line 1: | ||
| - | [[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== | ||
| Line 13: | Line 13: | ||
[[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
|
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 Thu Feb 21 17:20:45 2008
