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'''THE CO-FACTOR-INDUCED PRE-ACTIVE CONFORMATION IN PHOB''' | '''THE CO-FACTOR-INDUCED PRE-ACTIVE CONFORMATION IN PHOB''' | ||
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[[Category: Gomis-Ruth, F X.]] | [[Category: Gomis-Ruth, F X.]] | ||
[[Category: Sola, M.]] | [[Category: Sola, M.]] | ||
[[Category: | [[Category: Activation of the pho regulon]] | ||
[[Category: | [[Category: Activator]] | ||
[[Category: | [[Category: Alpha/beta doubly wound fold]] | ||
[[Category: | [[Category: Dna- binding]] | ||
[[Category: | [[Category: Dna-binding]] | ||
[[Category: | [[Category: Gene regulation]] | ||
[[Category: | [[Category: Phosphate regulation]] | ||
[[Category: | [[Category: Phosphate transport]] | ||
[[Category: | [[Category: Phosphorylation]] | ||
[[Category: | [[Category: Sensory transduction]] | ||
[[Category: | [[Category: Transcription]] | ||
[[Category: | [[Category: Transcription factor]] | ||
[[Category: | [[Category: Transcription regulation]] | ||
[[Category: | [[Category: Transport]] | ||
[[Category: | [[Category: Two-component regulatory system]] | ||
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Revision as of 08:05, 4 May 2008
THE CO-FACTOR-INDUCED PRE-ACTIVE CONFORMATION IN PHOB
OverviewOverview
PhoB is an Escherichia coli transcription factor from a two-component signal transduction system that is sensitive to limiting environmental phosphate conditions. It consists of an N-terminal receiver domain (RD) and a C-terminal DNA-binding domain. The protein is activated upon phosphorylation at the RD, an event that depends on Mg(2+) binding. The structure of PhoB RD in complex with Mg(2+) is presented, which shows three protomers in the asymmetric unit that interact across two different surfaces. One association is symmetric and has been described as a non-active dimerization contact; the other involves the alpha4-beta5-alpha5 interface and recalls the contact found in activated PhoB. However, here this last interaction is not perfectly symmetric and helix alpha4, which in the activated molecule undergoes a helical shift, becomes strongly destabilized in one of the interacting monomers. All protomers bind the cation in a similar manner but, interestingly, at the prospective binding site for the phosphate moiety the side chains of either Glu88 (in helix alpha4) or Trp54 alternate and interact with active-site atoms. When Glu88 is inside the cavity, helix alpha4 is arranged similarly to the unliganded wild-type structure. However, if Trp54 is present, the helix loses its contacts with the active-site cavity and vanishes. Accordingly, the presence of Trp54 in the active site induces a flexible state in helix alpha4, potentially allowing a helical shift that phosphorylation would eventually stabilize.
About this StructureAbout this Structure
2IYN is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
The cofactor-induced pre-active conformation in PhoB., Sola M, Drew DL, Blanco AG, Gomis-Ruth FX, Coll M, Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):1046-57. Epub 2006, Aug 19. PMID:16929106 Page seeded by OCA on Sun May 4 08:05:04 2008
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Escherichia coli
- Single protein
- Blanco, A G.
- Coll, M.
- Drew, D L.
- Gomis-Ruth, F X.
- Sola, M.
- Activation of the pho regulon
- Activator
- Alpha/beta doubly wound fold
- Dna- binding
- Dna-binding
- Gene regulation
- Phosphate regulation
- Phosphate transport
- Phosphorylation
- Sensory transduction
- Transcription
- Transcription factor
- Transcription regulation
- Transport
- Two-component regulatory system