PDBsum entry 1jbe

Signaling protein

PDB id: 1jbe

Contents

Protein chain

128 a.a. *

Ligands

SO4 ×3

GOL ×2

Waters ×199

* Residue conservation analysis

PDB id:

1jbe

Name:

Signaling protein

Title:

1.08 a structure of apo-chey reveals meta-active conformation

Structure:

Chemotaxis protein chey. Chain: a. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.08Å R-factor: 0.113 R-free: 0.152

Authors:

M.Simonovic,K.Volz

Key ref:

M.Simonovic and K.Volz (2001). A distinct meta-active conformation in the 1.1-A resolution structure of wild-type ApoCheY. J Biol Chem, 276, 28637-28640. PubMed id: 11410584 DOI: 10.1074/jbc.C100295200

Date:

04-Jun-01 Release date: 08-Aug-01

Protein chain

P0AE67  (CHEY_ECOLI) -  Chemotaxis protein CheY from Escherichia coli (strain K12)

Seq: 129 a.a.

Struc: 128 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1074/jbc.C100295200

J Biol Chem 276:28637-28640 (2001)

PubMed id: 11410584

A distinct meta-active conformation in the 1.1-A resolution structure of wild-type ApoCheY.

M.Simonovic, K.Volz.

ABSTRACT

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.

Selected figure(s)

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.

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.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2001, 276, 28637-28640) copyright 2001.