1SCM

STRUCTURE OF THE REGULATORY DOMAIN OF SCALLOP MYOSIN AT 2.8 ANGSTROMS RESOLUTION

Summary for 1SCM

• Entry DOI: 10.2210/pdb1scm/pdb
• Descriptor: MYOSIN HEAVY CHAIN, MYOSIN REGULATORY LIGHT CHAIN, MYOSIN ESSENTIAL LIGHT CHAIN, ... (4 entities in total)
• Functional Keywords: calcium-binding protein
• Biological source: Argopecten irradians; More
• Cellular location: Cytoplasm, myofibril: P24733
• Total number of polymer chains: 3
• Total formula weight: 40871.50

Authors

Cohen, C.,Xie, X. (deposition date: 1994-01-06, release date: 1994-04-30, Last modification date: 2024-02-14)

Primary citation

Xie, X.,Harrison, D.H.,Schlichting, I.,Sweet, R.M.,Kalabokis, V.N.,Szent-Gyorgyi, A.G.,Cohen, C.
Structure of the regulatory domain of scallop myosin at 2.8 A resolution.
Nature, 368:306-312, 1994

PubMed Abstract: 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.

PubMed: 8127365
DOI: 10.1038/368306a0

Experimental method

X-RAY DIFFRACTION (2.8 Å)