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PDBsum entry 1jbe
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Signaling protein
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PDB id
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1jbe
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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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A distinct meta-Active conformation in the 1.1-A resolution structure of wild-Type apochey.
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Authors
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M.Simonovic,
K.Volz.
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Ref.
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J Biol Chem, 2001,
276,
28637-28640.
[DOI no: ]
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PubMed id
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Abstract
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CheY is the best characterized member of the response regulator superfamily, and
as such it has become the principal model for understanding the initial
molecular mechanisms of signaling in two-component systems. Normal signaling by
response regulators requires phosphorylation, in combination with an activation
mechanism whose conformational effects are not completely understood. CheY
activation involves three events, phosphorylation, a conformational change in
the beta(4)--alpha(4) loop, and a rotational restriction of the side chain of
tyrosine 106. An outstanding question concerns the nature of an active
conformation in the apoCheY population. The details of this 1.08-A resolution
crystal structure of wild-type apoCheY shows the beta(4)--alpha(4) loop in two
distinctly different conformations that sterically correlate with the two
rotameric positions of the tyrosine 106 side chain. One of these conformational
states of CheY is the inactive form, and we propose that the other is a
meta-active form, responsible for the active properties seen in apoCheY.
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Figure 1.
Fig. 1. Stereo diagram showing the structural details of
the conformational heterogeneity of the  [4]-  [4] loop
and the Tyr106 side chain of wild-type apoCheY. The omit |F[o
 ]F[c]|
[c]
electron density is contoured at 3.5  . A,
alanine; Y, tyrosine.
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Figure 2.
Fig. 2. Schematic diagram for the four possible combined
conformations of the [4]- [4] loop
and the Tyr106 side chain of wild-type apoCheY. Y, tyrosine.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2001,
276,
28637-28640)
copyright 2001.
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Secondary reference #1
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Title
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Atomic resolution structure of a succinimide intermediate in e.Coli chey.
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Authors
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M.Simonovic,
K.Volz.
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Ref.
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J Mol Biol, 2002,
322,
663-667.
[DOI no: ]
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PubMed id
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Figure 1.
Figure 1. (a) Stereo view of the final |2F[o] -F[c]|a[c]
electron density map of the succinimide ring formed in the
a[3]-b[4] loop of CheY between residues Asp75 and Gly76,
contoured at 2.5s. The succinimide residue is labeled as Snn75,
while the following acetyl group is labeled as Acy76. (b)
Structural formula of the Image -succinimide showing atom
labeling used in the Snn-Acy group. CH3 is the full name of the
bridging carbon between N1 and the carbonyl carbon; H3 does not
refer to any hydrogen atoms.
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Figure 3.
Figure 3. Stereo view of the bonding interaction between
the O3 atom of the sulfate ion and the N1 atom of the
succinimide residue. The |2F[o] -F[c]|a[c] electron density map
is contoured at 2.5s.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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