Crystal Structure of a Phosphorylated Light Chain Domain of Scallop Smooth-Muscle Myosin

We have determined the crystal structure of a phosphorylated smooth-muscle myosin light chain domain (LCD). This reconstituted LCD is of a sea scallop catch muscle myosin with its phosphorylatable regulatory light chain (RLC SmoA). In the crystal structure, Arg16, an arginine residue that is present...

Full description

Saved in:
Bibliographic Details
Published in:Biophysical journal 2011-11, Vol.101 (9), p.2185-2189
Main Authors: Senthil Kumar, V.S., O'Neall-Hennessey, Elizabeth, Reshetnikova, Ludmila, Brown, Jerry H., Robinson, Howard, Szent-Györgyi, Andrew G., Cohen, Carolyn
Format: Article
Language:English
Subjects:
60 APPLIED LIFE SCIENCES
Amino Acid Sequence
Amino acids
Animals
ARGININE
BASIC BIOLOGICAL SCIENCES
CARBONYLS
Cells
CHAINS
CRYSTAL STRUCTURE
Crystal surfaces
Crystallization
Crystallography, X-Ray
Molecular Sequence Data
Muscle, Motility, and Motor Proteins
MUSCLES
MYOSIN
myosin light chains
Myosin Light Chains - chemistry
Pectinidae - metabolism
PHOSPHATES
PHOSPHORYLATION
Placopecten magellanicus
Protein Structure, Tertiary
Proteins
REGULATIONS
RESIDUES
scallops
SEAS
SERINE
smooth muscle
Smooth Muscle Myosins - chemistry
VERTEBRATES
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:We have determined the crystal structure of a phosphorylated smooth-muscle myosin light chain domain (LCD). This reconstituted LCD is of a sea scallop catch muscle myosin with its phosphorylatable regulatory light chain (RLC SmoA). In the crystal structure, Arg16, an arginine residue that is present in this isoform but not in vertebrate smooth-muscle RLC, stabilizes the phosphorylation site. This arginine interacts with the carbonyl group of the phosphorylation-site serine in the unphosphorylated LCD (determined previously), and with the phosphate group when the serine is phosphorylated. However, the overall conformation of the LCD is essentially unchanged upon phosphorylation. This result provides additional evidence that phosphorylation of the RLC is unlikely to act as an on-switch in regulation of scallop catch muscle myosin.
ISSN:0006-3495
1542-0086
DOI:10.1016/j.bpj.2011.09.028