caa a22 4500 39755608X CHVBK 20180308164802.0 cr unu---uuuuu 161202e199606 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021346 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021346 Secondary Structure and Ca2+-Binding Property of the N-Terminal Half Domain of Calmodulin from Yeast Saccharomyces cerevisiae as Studied by NMR [Elektronische Daten] [Shin-ya Ohki, Kazunori Miura, Moyoko Saito, Ken-ichi Nakashima, Hironobu Maekawa, Michio Yazawa, Sakae Tsuda, Kunio Hikichi] Using two- and three-dimensional NMR techniques, 1H and main-chain 15N resonances of the N-terminal half domain of yeast calmodulin (YCMO-N) in the presence of Mg2+ and Ca2+ (Mg2+- and Ca2+-forms) were assigned. The secondary structures of YCMO-N in both forms were determined. The NOESY and 15N-edited NOESY spectra of YCMO-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 YCMO-N in the Mg2+-form. The B-helix is, however, not formed in the Ca2+-form. The Ca2+-binding of YCMO-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. © by the Journal of Biochemistry Regular Papers nationallicence Ca2+-induced conformational change nationallicence NMRN-domain of yeast calmodulin nationallicence secondary structure nationallicence Ohki Shin-ya High-Resolution NMR Laboratory N10-W8, Kita-ku, Sapporo 060 aut Miura Kazunori Divisions of Biological Sciences N10-W8, Kita-ku, Sapporo 060 aut Saito Moyoko Divisions of Biological Sciences N10-W8, Kita-ku, Sapporo 060 aut Nakashima Ken-ichi Chemistry, Graduate School of Science, Hokkaido University N10-W8, Kita-ku, Sapporo 060 aut Maekawa Hironobu Chemistry, Graduate School of Science, Hokkaido University N10-W8, Kita-ku, Sapporo 060 aut Yazawa Michio Chemistry, Graduate School of Science, Hokkaido University N10-W8, Kita-ku, Sapporo 060 aut Tsuda Sakae Bioscience and Chemistry Division, Hokkaido National Industrial Research Institute 2-17-2-1 Tsukisamu-higashi, Toyohira-ku, Sapporo 062 aut Hikichi Kunio High-Resolution NMR Laboratory N10-W8, Kita-ku, Sapporo 060 aut The Journal of Biochemistry Oxford University Press 119/6(1996-06), 1045-1055 0021-924X 119:6<1045 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021346 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021346 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Ohki Shin-ya High-Resolution NMR Laboratory N10-W8, Kita-ku, Sapporo 060 aut NATIONALLICENCE 700 1- Miura Kazunori Divisions of Biological Sciences N10-W8, Kita-ku, Sapporo 060 aut NATIONALLICENCE 700 1- Saito Moyoko Divisions of Biological Sciences N10-W8, Kita-ku, Sapporo 060 aut NATIONALLICENCE 700 1- Nakashima Ken-ichi Chemistry, Graduate School of Science, Hokkaido University N10-W8, Kita-ku, Sapporo 060 aut NATIONALLICENCE 700 1- Maekawa Hironobu Chemistry, Graduate School of Science, Hokkaido University N10-W8, Kita-ku, Sapporo 060 aut NATIONALLICENCE 700 1- Yazawa Michio Chemistry, Graduate School of Science, Hokkaido University N10-W8, Kita-ku, Sapporo 060 aut NATIONALLICENCE 700 1- Tsuda Sakae Bioscience and Chemistry Division, Hokkaido National Industrial Research Institute 2-17-2-1 Tsukisamu-higashi, Toyohira-ku, Sapporo 062 aut NATIONALLICENCE 700 1- Hikichi Kunio High-Resolution NMR Laboratory N10-W8, Kita-ku, Sapporo 060 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/6(1996-06), 1045-1055 0021-924X 119:6<1045 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford