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H-1, n-15, and c-13 backbone chemical-shift assignments, secondary structure, and magnesium-binding characteristics of the bacillus-subtilis response regulator, spoof, determined by heteronuclear high-resolution NMR

Academic Article
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Overview

authors

  • Feher, V. A.
  • Zapf, J. W.
  • Hoch, James
  • Dahlquist, F. W.
  • Whiteley, J. M.
  • Cavanagh, J.

publication date

  • 1995

journal

  • Protein Science  Journal

abstract

  • Spo0F, sporulation stage 0 F protein, a 124-residue protein responsible, in part, for regulating the transition of Bacillus subtilis from a vegetative state to a dormant endospore, has been studied by high-resolution NMR. The 1H, 15N, and 13C chemical shift assignments for the backbone residues have been determined from analyses of 3D spectra, 15N TOCSY-HSQC, 15N NOESY-HSQC, HNCA, and HN(CO)CA. Assignments for many sidechain proton resonances are also reported. The secondary structure, inferred from short- and medium-range NOEs, 3JHN alpha coupling constants, and hydrogen exchange patterns, define a topology consistent with a doubly wound (alpha/beta)5 fold. Interestingly, comparison of the secondary structure of Spo0F to the structure of the Escherichia coli response regulator, chemotaxis Y protein (CheY) (Volz K, Matsumura P, 1991, J Biol Chem 266:15511-15519; Bruix M et al., 1993, Eur J Biochem 215:573-585), show differences in the relative length of secondary structure elements that map onto a single face of the tertiary structure of CheY. This surface may define a region of binding specificity for response regulators. Magnesium titration of Spo0F, followed by amide chemical shift changes, gives an equilibrium dissociation constant of 20 +/- 5 mM. Amide resonances most perturbed by magnesium binding are near the putative site of phosphorylation, Asp 54.

subject areas

  • Amino Acid Sequence
  • Bacillus subtilis
  • Bacterial Proteins
  • Binding Sites
  • Carbon Isotopes
  • Escherichia coli
  • Hydrogen
  • Magnesium
  • Magnetic Resonance Spectroscopy
  • Membrane Proteins
  • Molecular Sequence Data
  • Nitrogen Isotopes
  • Phosphorylation
  • Protein Structure, Secondary
  • Signal Transduction
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Research

keywords

  • 2-COMPONENT SIGNALING SYSTEMS
  • BACTERIAL SIGNAL TRANSDUCTION
  • CHEY
  • PHOSPHO-RELAY
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Identity

PubMed Central ID

  • PMC2143210

International Standard Serial Number (ISSN)

  • 0961-8368

Digital Object Identifier (DOI)

  • 10.1002/pro.5560040915

PubMed ID

  • 8528078
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Additional Document Info

start page

  • 1801

end page

  • 1814

volume

  • 4

issue

  • 9

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