PDBsum entry: 1f4v

Signaling protein

PDB id: 1f4v

Contents

Protein chains

128 a.a. *

16 a.a. *

14 a.a. *

Ligands

BEF ×3

GOL ×2

Metals

_MG ×3

Waters ×280

* Residue conservation analysis

PDB id:

1f4v

Name:

Signaling protein

Title:

Crystal structure of activated chey bound to the n-terminus

Structure:

Chemotaxis chey protein. Chain: a, b, c. Engineered: yes. Flagellar motor switch protein. Chain: d, e, f. Fragment: n-terminus. Synonym: flim

Source:

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

Biol. unit:

Dodecamer (from PQS)

Resolution:

2.22Å R-factor: 0.217 R-free: 0.258

Authors:

S.Y.Lee,H.S.Cho,J.G.Pelton,D.Yan,R.K.Henderson,D.King,L.S.Hu S.Kustu,E.A.Berry,D.E.Wemmer

Key ref:

S.Y.Lee et al. (2001). Crystal structure of an activated response regulator bound to its target. Nat Struct Biol, 8, 52-56. PubMed id: 11135671 DOI: 10.1038/83053

Date:

10-Jun-00 Release date: 17-Jan-01

Protein chains

P0AE67  (CHEY_ECOLI) -  Chemotaxis protein CheY

Seq: 129 a.a.

Struc: 128 a.a.

Protein chain

P06974  (FLIM_ECOLI) -  Flagellar motor switch protein FliM

Seq: 334 a.a.

Struc: 16 a.a.

Protein chains

P06974  (FLIM_ECOLI) -  Flagellar motor switch protein FliM

Seq: 334 a.a.

Struc: 14 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: cytoplasm (1 term)
• Biological process: intracellular signal transduction (7 terms)
• Biochemical function: two-component response regulator activity (3 terms)

DOI no: 10.1038/83053

Nat Struct Biol 8:52-56 (2001)

PubMed id: 11135671

Crystal structure of an activated response regulator bound to its target.

S.Y.Lee, H.S.Cho, J.G.Pelton, D.Yan, R.K.Henderson, D.S.King, L.Huang, S.Kustu, E.A.Berry, D.E.Wemmer.

ABSTRACT

The chemotactic regulator CheY controls the direction of flagellar rotation in Escherichia coli. We have determined the crystal structure of BeF3--activated CheY from E. coli in complex with an N-terminal peptide derived from its target, FliM. The structure reveals that the first seven residues of the peptide pack against the beta4-H4 loop and helix H4 of CheY in an extended conformation, whereas residues 8-15 form two turns of helix and pack against the H4-beta5-H5 face. The peptide binds the only region of CheY that undergoes noticeable conformational change upon activation and would most likely be sandwiched between activated CheY and the remainder of FliM to reverse the direction of flagellar rotation.

Selected figure(s)

Figure 2.
Figure 2. Stereo view of the active site of CheY showing the F[o] - F[c] electron density for the BeF[3]^- moiety contoured at 5.5 . This map was calculated with the occupancy of the BeF[3]^- moiety set to zero. The three F atoms, shown in light blue, adopt a tetrahedral geometry around Be and hydrogen bond with the hydroxyl group of Thr 87, N of Lys 109 and backbone amides of Ala 88 and Asn 59. BeF[3]^- also serves as a ligand for Mg2+ (dark green). The two water molecules that coordinate with Mg2+ are shown in red. Carbon, nitrogen, and oxygen atoms are shown in green, dark blue, and red, respectively. For additional interactions see the text.

Figure 3.
Figure 3. GRASP33 electrostatic surface representations of: a, apo-CheY with Tyr 106 in the solvent exposed position34; b, CheY alone from the CheY -N16-FliM complex; c, the CheY -N16-FliM complex. Comparison of (a) and (b) shows that Tyr 106 in the solvent exposed position sterically interferes with peptide binding to the H4- 5-H5 face.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2001, 8, 52-56) copyright 2001.

Figures were selected by an automated process.