title: Conformational dynamics of yeast calmodulin in the Ca(2+)-bound state probed using NMR relaxation dispersion.
abstract: Most calmodulin (CaM) in apo and Ca(2+)-bound states show a dumb-bell-like structure, involving the N- and C-terminal domains, connected with a flexible linker. However, Ca(2+)-bound yeast calmodulin (yCaM) takes on a unique globular structure; the target-binding site of this protein is autoinhibited. We applied NMR relaxation dispersion experiments to yCaM in the Ca(2+)-bound state. The amide (15)N and (1)H(N) relaxation dispersion profiles indicated the presence of conformational dynamics for specific residues at the interface between the N- and C-terminal domains. We conclude that these conformational dynamics were derived from the mobility of the C-terminal domain.
authors: Department of Structural Biology, Faculty of Advanced Life Science, Hokkaido University, Kita 21 Nishi 11, Sapporo 001-0021, Japan. k-ogura@mail.sci.hokudai.ac.jp
authors: Kenji
authors: K
authors: Ogura
authors: Hideyasu
authors: H
authors: Okamura
authors: Masato
authors: M
authors: Katahira
authors: Etsuko
authors: E
authors: Katoh
authors: Fuyuhiko
authors: F
authors: Inagaki
mesh_terms: D000465:Algorithms; D000577:Amides / Q000737:chemistry; D020816:Amino Acid Motifs; D001665:Binding Sites; D002118:Calcium / Q000737:chemistry*; D002147:Calmodulin / Q000737:chemistry*; D004926:Escherichia coli / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008958:Models, Molecular; D015233:Models, Statistical; D009154:Mutation; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D015203:Reproducibility of Results; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D013997:Time Factors
chemical_list: D000577:Amides; D002147:Calmodulin; D010455:Peptides; D002118:Calcium