2iyn

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|PDB= 2iyn |SIZE=350|CAPTION= <scene name='initialview01'>2iyn</scene>, resolution 2.08&Aring;
|PDB= 2iyn |SIZE=350|CAPTION= <scene name='initialview01'>2iyn</scene>, resolution 2.08&Aring;
|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+C'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+C'>AC1</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iyn OCA], [http://www.ebi.ac.uk/pdbsum/2iyn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iyn RCSB]</span>
}}
}}
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[[Category: Gomis-Ruth, F X.]]
[[Category: Gomis-Ruth, F X.]]
[[Category: Sola, M.]]
[[Category: Sola, M.]]
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[[Category: MG]]
 
[[Category: activation of the pho regulon]]
[[Category: activation of the pho regulon]]
[[Category: activator]]
[[Category: activator]]
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[[Category: two-component regulatory system]]
[[Category: two-component regulatory system]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:35:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:50:32 2008''

Revision as of 00:50, 31 March 2008

Image:2iyn.gif


PDB ID 2iyn

Drag the structure with the mouse to rotate
, resolution 2.08Å
Sites:
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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

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