1ffw: Difference between revisions

Revision as of 13:38, 21 February 2008

CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY WITH A BOUND IMIDO DIPHOSPHATE

OverviewOverview

New crystallographic structures of the response regulator CheY in association with CheA(124--257), its binding domain in the kinase CheA, have been determined. In all crystal forms, the molecular interactions at the heterodimer interface are identical. Soaking experiments have been performed on the crystals using acetyl phosphate as phosphodonor to CheY. No phosphoryl group attached to Asp57 of CheY is visible from the electron density, but the response regulator in the CheY-CheA(124--257) complex may have undergone a phosphorylation-dephosphorylation process. The distribution of water molecules and the geometry of the active site have changed and are now similar to those of isolated CheY. In a second soaking experiment, imido-diphosphate, an inhibitor of the phosphorylation reaction, was used. This compound binds in the vicinity of the active site, close to the N-terminal part of the first alpha-helix. Together, these results suggest that the binding of CheY to CheA(124--257) generates a geometry of the active site that favours phosphorylation and that imido-diphosphate interferes with phosphorylation by precluding structural changes in this region.

About this StructureAbout this Structure

1FFW is a Protein complex structure of sequences from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

Further insights into the mechanism of function of the response regulator CheY from crystallographic studies of the CheY--CheA(124--257) complex., Gouet P, Chinardet N, Welch M, Guillet V, Cabantous S, Birck C, Mourey L, Samama JP, Acta Crystallogr D Biol Crystallogr. 2001 Jan;57(Pt 1):44-51. PMID:11134926

Page seeded by OCA on Thu Feb 21 12:38:12 2008

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OCA

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-[[Image:1ffw.jpg|left|200px]]<br /><applet load="1ffw" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1ffw, resolution 2.7&Aring;" />
 '''CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY WITH A BOUND IMIDO DIPHOSPHATE'''<br />
 ==Overview==
-New crystallographic structures of the response regulator CheY in, association with CheA(124--257), its binding domain in the kinase CheA, have been determined. In all crystal forms, the molecular interactions at, the heterodimer interface are identical. Soaking experiments have been, performed on the crystals using acetyl phosphate as phosphodonor to CheY., No phosphoryl group attached to Asp57 of CheY is visible from the electron, density, but the response regulator in the CheY-CheA(124--257) complex may, have undergone a phosphorylation-dephosphorylation process. The, distribution of water molecules and the geometry of the active site have, changed and are now similar to those of isolated CheY. In a second soaking, experiment, imido-diphosphate, an inhibitor of the phosphorylation, reaction, was used. This compound binds in the vicinity of the active, site, close to the N-terminal part of the first alpha-helix. Together, these results suggest that the binding of CheY to CheA(124--257) generates, a geometry of the active site that favours phosphorylation and that, imido-diphosphate interferes with phosphorylation by precluding structural, changes in this region.
+New crystallographic structures of the response regulator CheY in association with CheA(124--257), its binding domain in the kinase CheA, have been determined. In all crystal forms, the molecular interactions at the heterodimer interface are identical. Soaking experiments have been performed on the crystals using acetyl phosphate as phosphodonor to CheY. No phosphoryl group attached to Asp57 of CheY is visible from the electron density, but the response regulator in the CheY-CheA(124--257) complex may have undergone a phosphorylation-dephosphorylation process. The distribution of water molecules and the geometry of the active site have changed and are now similar to those of isolated CheY. In a second soaking experiment, imido-diphosphate, an inhibitor of the phosphorylation reaction, was used. This compound binds in the vicinity of the active site, close to the N-terminal part of the first alpha-helix. Together, these results suggest that the binding of CheY to CheA(124--257) generates a geometry of the active site that favours phosphorylation and that imido-diphosphate interferes with phosphorylation by precluding structural changes in this region.
 ==About this Structure==
-FFW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MN and PON as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FFW OCA].
+FFW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=PON:'>PON</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FFW OCA].
 ==Reference==
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 [[Category: doubly wound (beta/alpha)5 fold]]
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