3TS5: Crystal Structure Of A Light Chain Domain Of Scallop Smooth Muscle Myosin

Citation:
Abstract
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, Arg(16), 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.
PDB ID: 3TS5Download
MMDB ID: 95271
PDB Deposition Date: 2011/9/12
Updated in MMDB: 2011/11
Experimental Method:
x-ray diffraction
Resolution: 2.39  Å
Source Organism:
Similar Structures:
Biological Unit for 3TS5: trimeric; determined by author and by software (PISA)
Molecular Components in 3TS5
Label Count Molecule
Proteins (3 molecules)
1
Myosin Heavy Chain
Molecule annotation
1
Myosin Regulatory Light Chain
Molecule annotation
1
Myosin Essential Light Chain
Molecule annotation
Chemicals (2 molecules)
1
1
2
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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