Structure of the regulatory domain of scallop myosin at 2.8 A resolution.
The regulatory domain of scallop myosin is a three-chain protein complex that switches on this motor in response to Ca2+ binding. This domain has been crystallized and the structure solved to 2.8 A resolution. Side-chain interactions link the two light chains in tandem to adjacent segments of the heavy chain bearing the IQ-sequence motif. The Ca(2+)-binding site is a novel EF-hand motif on the essential light chain and is stabilized by linkages involving the heavy chain and both light chains, accounting for the requirement of all three chains for Ca2+ binding and regulation in the intact myosin molecule.
Xie
X
X
Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02254-9110.
Harrison
D H
DH
Schlichting
I
I
Sweet
R M
RM
Kalabokis
V N
VN
Szent-Györgyi
A G
AG
Cohen
C
C
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000378:metabolism; D003196:Computer Graphics; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D008974:Mollusca; D009218:Myosins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation
D010446:Peptide Fragments; D009218:Myosins; D002118:Calcium