Secondary structure and Ca(2+)-binding property of the N-terminal half domain of calmodulin from yeast Saccharomyces cerevisiae as studied by NMR
| Autor: | Kazunori Miura, Moyoko Saito, Hironobu Maekawa, Michio Yazawa, Kunio Hikichi, Sakae Tsuda, Ken-ichi Nakashima, Shin-ya Ohki |
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| Rok vydání: | 1996 |
| Předmět: |
chemistry.chemical_classification
Magnetic Resonance Spectroscopy Calmodulin Saccharomyces cerevisiae Molecular Sequence Data General Medicine Nuclear magnetic resonance spectroscopy Biology biology.organism_classification Antiparallel (biochemistry) Biochemistry Protein Structure Secondary Amino acid Crystallography chemistry biology.protein Calcium Magnesium Amino Acid Sequence Molecular Biology Peptide sequence Two-dimensional nuclear magnetic resonance spectroscopy Protein secondary structure |
| Zdroj: | Journal of biochemistry. 119(6) |
| ISSN: | 0021-924X |
| Popis: | 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+ (Mg(2+)-and Ca(2+)-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 Ca(2+)-binding loops are connected by a short antiparallel beta-sheet. There are four helices (A, B, C, and D named from the N-terminus) for YCM0-N in the Mg(2+)-form. The B-helix is, however, not formed in the Ca(2+)-form. The Ca(2+)-binding of YCM0-N was monitored by (1H,15N)-HSQC at various Ca2+ concentrations. The observed spectral changes as a function of Ca(2+)-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. |
| Databáze: | OpenAIRE |
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