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Crystal structure of activated CheY. Comparison with other activated receiver domains.

Publication ,  Journal Article
Lee, SY; Cho, HS; Pelton, JG; Yan, D; Berry, EA; Wemmer, DE
Published in: J Biol Chem
May 11, 2001

The crystal structure of BeF(3)(-)-activated CheY, with manganese in the magnesium binding site, was determined at 2.4-A resolution. BeF(3)(-) bonds to Asp(57), the normal site of phosphorylation, forming a hydrogen bond and salt bridge with Thr(87) and Lys(109), respectively. The six coordination sites for manganese are satisfied by a fluorine of BeF(3)(-), the side chain oxygens of Asp(13) and Asp(57), the carbonyl oxygen of Asn(59), and two water molecules. All of the active site interactions seen for BeF(3)(-)-CheY are also observed in P-Spo0A(r). Thus, BeF(3)(-) activates CheY as well as other receiver domains by mimicking both the tetrahedral geometry and electrostatic potential of a phosphoryl group. The aromatic ring of Tyr(106) is found buried within a hydrophobic pocket formed by beta-strand beta4 and helix H4. The tyrosine side chain is stabilized in this conformation by a hydrogen bond between the hydroxyl group and the backbone carbonyl oxygen of Glu(89). This hydrogen bond appears to stabilize the active conformation of the beta4/H4 loop. Comparison of the backbone coordinates for the active and inactive states of CheY reveals that only modest changes occur upon activation, except in the loops, with the largest changes occurring in the beta4/H4 loop. This region is known to be conformationally flexible in inactive CheY and is part of the surface used by activated CheY for binding its target, FliM. The pattern of activation-induced backbone coordinate changes is similar to that seen in FixJ(r). A common feature in the active sites of BeF(3)(-)-CheY, P-Spo0A(r), P-FixJ(r), and phosphono-CheY is a salt bridge between Lys(109) Nzeta and the phosphate or its equivalent, beryllofluoride. This suggests that, in addition to the concerted movements of Thr(87) and Tyr(106) (Thr-Tyr coupling), formation of the Lys(109)-PO(3)(-) salt bridge is directly involved in the activation of receiver domains generally.

Duke Scholars

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

May 11, 2001

Volume

276

Issue

19

Start / End Page

16425 / 16431

Location

United States

Related Subject Headings

  • Recombinant Proteins
  • Protein Structure, Secondary
  • Models, Molecular
  • Methyl-Accepting Chemotaxis Proteins
  • Membrane Proteins
  • Manganese
  • Magnesium
  • Escherichia coli Proteins
  • Escherichia coli
  • Crystallography, X-Ray
 

Citation

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Lee, S. Y., Cho, H. S., Pelton, J. G., Yan, D., Berry, E. A., & Wemmer, D. E. (2001). Crystal structure of activated CheY. Comparison with other activated receiver domains. J Biol Chem, 276(19), 16425–16431. https://doi.org/10.1074/jbc.M101002200
Lee, S. Y., H. S. Cho, J. G. Pelton, D. Yan, E. A. Berry, and D. E. Wemmer. “Crystal structure of activated CheY. Comparison with other activated receiver domains.J Biol Chem 276, no. 19 (May 11, 2001): 16425–31. https://doi.org/10.1074/jbc.M101002200.
Lee SY, Cho HS, Pelton JG, Yan D, Berry EA, Wemmer DE. Crystal structure of activated CheY. Comparison with other activated receiver domains. J Biol Chem. 2001 May 11;276(19):16425–31.
Lee, S. Y., et al. “Crystal structure of activated CheY. Comparison with other activated receiver domains.J Biol Chem, vol. 276, no. 19, May 2001, pp. 16425–31. Pubmed, doi:10.1074/jbc.M101002200.
Lee SY, Cho HS, Pelton JG, Yan D, Berry EA, Wemmer DE. Crystal structure of activated CheY. Comparison with other activated receiver domains. J Biol Chem. 2001 May 11;276(19):16425–16431.

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

May 11, 2001

Volume

276

Issue

19

Start / End Page

16425 / 16431

Location

United States

Related Subject Headings

  • Recombinant Proteins
  • Protein Structure, Secondary
  • Models, Molecular
  • Methyl-Accepting Chemotaxis Proteins
  • Membrane Proteins
  • Manganese
  • Magnesium
  • Escherichia coli Proteins
  • Escherichia coli
  • Crystallography, X-Ray