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PDBsum entry 1ffs
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Transferase/signaling protein
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PDB id
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1ffs
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Further insights into the mechanism of function of the response regulator chey from crystallographic studies of the chey--Chea(124--257) complex.
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Authors
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P.Gouet,
N.Chinardet,
M.Welch,
V.Guillet,
S.Cabantous,
C.Birck,
L.Mourey,
J.P.Samama.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2001,
57,
44-51.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 3.
Figure 3 Close-up view at the heterodimer interface illustrating
the environment of Tyr106 in CheY and of Glu178, His181 and
Phe214 in P2. The 2F[o] - F[c] map of the 2.1 Å resolution
native structure is contoured at 1  .
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Figure 5.
Figure 5 Stereoview of the bound imido-diphosphate and its
network of electrostatic interactions. The 2.7 Å 2F[o] - F[c]
map is contoured at 1 .
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2001,
57,
44-51)
copyright 2001.
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Secondary reference #1
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Title
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Structure of the chey-Binding domain of histidine kinase chea in complex with chey.
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Authors
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M.Welch,
N.Chinardet,
L.Mourey,
C.Birck,
J.P.Samama.
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Ref.
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Nat Struct Biol, 1998,
5,
25-29.
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PubMed id
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