2iyn
From Proteopedia
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==Overview== | ==Overview== | ||
| - | PhoB is an Escherichia coli transcription factor from a two-component | + | 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 Structure== | ==About this Structure== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Blanco, A | + | [[Category: Blanco, A G.]] |
[[Category: Coll, M.]] | [[Category: Coll, M.]] | ||
| - | [[Category: Drew, D | + | [[Category: Drew, D L.]] |
| - | [[Category: Gomis-Ruth, F | + | [[Category: Gomis-Ruth, F X.]] |
[[Category: Sola, M.]] | [[Category: Sola, M.]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: two-component regulatory system]] | [[Category: two-component regulatory system]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:57:31 2008'' |
Revision as of 15:57, 21 February 2008
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THE CO-FACTOR-INDUCED PRE-ACTIVE CONFORMATION IN PHOB
Overview
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 Structure
2IYN is a Single protein structure of sequence from Escherichia coli with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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 Thu Feb 21 17:57:31 2008
Categories: Escherichia coli | Single protein | Blanco, A G. | Coll, M. | Drew, D L. | Gomis-Ruth, F X. | Sola, M. | MG | 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
