Prokaryotic calcium-binding protein of the calmodulin superfamily. Calcium binding to a Saccharopolyspora erythraea 20 kDa protein

FEBS Lett. 1992 Mar 24;299(1):44-7. doi: 10.1016/0014-5793(92)80096-y.

Abstract

The EF-hand calcium-binding protein from Saccharopolyspora erythraea has been shown, using 113Cd NMR, to possess three Cd(2+)-ion binding sites. This indicates that of the four EF-hand motifs in the molecule, one (probably site 2) is unable to bind Cd(2+)-ions. Data from the titration of the protein with Ca2+, in the presence of Quin2, were fitted to a curve calculated on the assumption that the protein contains three high affinity Ca2+ binding sites, two of which (pK1 = 8.0, pK2 = 9.0) are strongly cooperative, and one single site (pK3 = 7.5). Preliminary 1H NMR experiments indicate marked structural changes upon Ca(2+)-binding.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Calcium / metabolism*
  • Calcium-Binding Proteins / chemistry
  • Calcium-Binding Proteins / classification
  • Calcium-Binding Proteins / metabolism*
  • Calmodulin / chemistry
  • Calmodulin / metabolism*
  • Fungal Proteins / chemistry
  • Fungal Proteins / classification
  • Fungal Proteins / metabolism
  • Magnetic Resonance Spectroscopy
  • Saccharopolyspora / metabolism*

Substances

  • Calcium-Binding Proteins
  • Calmodulin
  • Fungal Proteins
  • Calcium