3TS5

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

3TS5 の概要

• エントリーDOI: 10.2210/pdb3ts5/pdb
• 関連するPDBエントリー: 3PN7 3TUY
• 分子名称: Myosin heavy chain, Myosin regulatory light chain, Myosin essential light chain, ... (6 entities in total)
• 機能のキーワード: alpha helix, myosin regulation, catch muscle, structural protein
• 由来する生物種: Placopecten magellanicus (Sea scallop); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 89492.21

構造登録者

Kumar, V.S.S.,O'Neall-Hennessey, E.,Reshetnikova, L.,Brown, J.H.,Robinson, H.,Szent-Gyorgyi, A.G.,Cohen, C. (登録日: 2011-09-12, 公開日: 2011-11-23, 最終更新日: 2024-02-28)

主引用文献

Senthil Kumar, V.S.,O'Neall-Hennessey, E.,Reshetnikova, L.,Brown, J.H.,Robinson, H.,Szent-Gyorgyi, A.G.,Cohen, C.
Crystal structure of a phosphorylated light chain domain of scallop smooth-muscle Myosin.
Biophys.J., 101:2185-2189, 2011

PubMed 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.

PubMed: 22067157
DOI: 10.1016/j.bpj.2011.09.028

実験手法

X-RAY DIFFRACTION (2.393 Å)