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Conformational dynamics of yeast calmodulin in the Ca 2+ ‐bound state probed using NMR relaxation dispersion
Author(s) -
Ogura Kenji,
Okamura Hideyasu,
Katahira Masato,
Katoh Etsuko,
Inagaki Fuyuhiko
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.06.031
Subject(s) - calmodulin , relaxation (psychology) , chemistry , crystallography , linker , bound state , dispersion (optics) , molecular dynamics , yeast , biophysics , physics , calcium , biochemistry , computational chemistry , biology , organic chemistry , quantum mechanics , neuroscience , computer science , optics , operating system
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.