Secondary Structure and Ca^<2+>-Binding Property of the N-Terminal Half Domain of Calmodulin from Yeast Saccharomyces cerevisiae as Studied by NMR

OHKI Shin-ya, MIURA Kazunori, SAITO Moyoko, NAKASHIMA Ken-ichi, MAEKAWA Hironobu, YAZAWA Michio, TSUDA Sakae, HIKICHI Kunio

Using two- and three-dimensional NMR techniques, ¹H and main-chain ¹⁵N resonances of the N-terminal half domain of yeast calmodulin (YCM0-N) in the presence of Mg²⁺ and Ca²⁺ (Mg²⁺- and Ca²⁺-forms) were assigned. The secondary structures of YCM0-N in both forms were determined. The NOESY and ¹⁵N-edited NOESY spectra of YCM0-N in each form indicate that there is a hydrophobic core and that two Ca²⁺-binding loops are connected by a short antiparallel β-sheet. There are four helices (A, B, C, and D named from the N-terminus) for YCM0-N in the Mg²⁺-form. The B-helix is, however, not formed in the Ca²⁺-form. The Ca²⁺-binding of YCM0-N was monitored by (¹H, ¹⁵N)-HSQC at various Ca²⁺ concentrations. The observed spectral changes as a function of Ca²⁺-concentration can not readily be grouped into a small number of classes; each residue shows individual spectral change. There is no apparent relationship between the spectral change and the type or location of the amino acid concerned.

Secondary Structure and Ca^<2+>-Binding Property of the N-Terminal Half Domain of Calmodulin from Yeast Saccharomyces cerevisiae as Studied by NMR

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Secondary Structure and Ca^<2+>-Binding Property of the N-Terminal Half Domain of Calmodulin from Yeast Saccharomyces cerevisiae as Studied by NMR

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