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The NMR solution structure of BeF(3)(-)-activated Spo0F reveals the conformational switch in a phosphorelay system.

Publication ,  Journal Article
Gardino, AK; Volkman, BF; Cho, HS; Lee, S-Y; Wemmer, DE; Kern, D
Published in: J Mol Biol
August 1, 2003

Two-component systems, which are comprised of a single histidine-aspartate phosphotransfer module, are the dominant signaling pathways in bacteria and have recently been identified in several eukaryotic organisms as well. A tandem connection of two or more histidine-aspartate motifs forms complex phosphorelays. While response regulators from simple two-component systems have been characterized structurally in their inactive and active forms, we address here the question of whether a response regulator from a phosphorelay has a distinct structural basis of activation. We report the NMR solution structure of BeF(3)(-)-activated Spo0F, the first structure of a response regulator from a phosphorelay in its activated state. Conformational changes were found in regions previously identified to change in simple two-component systems. In addition, a downward shift by half a helical turn in helix 1, located on the opposite side of the common activation surface, was observed as a consequence of BeF(3)(-) activation. Conformational changes in helix 1 can be rationalized by the distinct function of phosphoryl transfer to the second histidine kinase, Spo0B, because helix 1 is known to interact directly with Spo0B and the phosphatase RapB. The identification of structural rearrangements in Spo0F supports the hypothesis of a pre-existing equilibrium between the inactive and active state prior to phosphorylation that was suggested on the basis of previous NMR dynamics studies on Spo0F. A shift of a pre-existing equilibrium is likely a general feature of response regulators.

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Published In

J Mol Biol

DOI

ISSN

0022-2836

Publication Date

August 1, 2003

Volume

331

Issue

1

Start / End Page

245 / 254

Location

Netherlands

Related Subject Headings

  • Signal Transduction
  • Protein Conformation
  • Phosphotransferases
  • Phosphorylation
  • Nuclear Magnetic Resonance, Biomolecular
  • Models, Molecular
  • Histidine
  • Fluorides
  • Biochemistry & Molecular Biology
  • Beryllium
 

Citation

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Gardino, A. K., Volkman, B. F., Cho, H. S., Lee, S.-Y., Wemmer, D. E., & Kern, D. (2003). The NMR solution structure of BeF(3)(-)-activated Spo0F reveals the conformational switch in a phosphorelay system. J Mol Biol, 331(1), 245–254. https://doi.org/10.1016/s0022-2836(03)00733-2
Gardino, Alexandra K., Brian F. Volkman, Ho S. Cho, Seok-Yong Lee, David E. Wemmer, and Dorothee Kern. “The NMR solution structure of BeF(3)(-)-activated Spo0F reveals the conformational switch in a phosphorelay system.J Mol Biol 331, no. 1 (August 1, 2003): 245–54. https://doi.org/10.1016/s0022-2836(03)00733-2.
Gardino AK, Volkman BF, Cho HS, Lee S-Y, Wemmer DE, Kern D. The NMR solution structure of BeF(3)(-)-activated Spo0F reveals the conformational switch in a phosphorelay system. J Mol Biol. 2003 Aug 1;331(1):245–54.
Gardino, Alexandra K., et al. “The NMR solution structure of BeF(3)(-)-activated Spo0F reveals the conformational switch in a phosphorelay system.J Mol Biol, vol. 331, no. 1, Aug. 2003, pp. 245–54. Pubmed, doi:10.1016/s0022-2836(03)00733-2.
Gardino AK, Volkman BF, Cho HS, Lee S-Y, Wemmer DE, Kern D. The NMR solution structure of BeF(3)(-)-activated Spo0F reveals the conformational switch in a phosphorelay system. J Mol Biol. 2003 Aug 1;331(1):245–254.
Journal cover image

Published In

J Mol Biol

DOI

ISSN

0022-2836

Publication Date

August 1, 2003

Volume

331

Issue

1

Start / End Page

245 / 254

Location

Netherlands

Related Subject Headings

  • Signal Transduction
  • Protein Conformation
  • Phosphotransferases
  • Phosphorylation
  • Nuclear Magnetic Resonance, Biomolecular
  • Models, Molecular
  • Histidine
  • Fluorides
  • Biochemistry & Molecular Biology
  • Beryllium