1MNE

TRUNCATED HEAD OF MYOSIN FROM DICTYOSTELIUM DISCOIDEUM COMPLEXED WITH MG-PYROPHOSPHATE

1MNE の概要

• エントリーDOI: 10.2210/pdb1mne/pdb
• 分子名称: MYOSIN, MAGNESIUM ION, PYROPHOSPHATE 2-, ... (4 entities in total)
• 機能のキーワード: atpase, myosin, coiled coil, actin-binding, atp-binding, heptad repeat pattern, methylation, alkylation, phosphorylation, contractile protein
• 由来する生物種: Dictyostelium discoideum
• 細胞内の位置: Cytoplasm, cell cortex: P08799
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 86949.27

構造登録者

Smith, C.A.,Rayment, I. (登録日: 1995-04-20, 公開日: 1996-08-17, 最終更新日: 2024-02-14)

主引用文献

Smith, C.A.,Rayment, I.
X-ray structure of the magnesium(II)-pyrophosphate complex of the truncated head of Dictyostelium discoideum myosin to 2.7 A resolution.
Biochemistry, 34:8973-8981, 1995

PubMed Abstract: The structure of the magnesium pyrophosphate complex of the truncated head of Dictyostelium myosin has been determined by molecular replacement at 2.7 A resolution and refined to a crystallographic R-factor of 16.0%. The crystals belong to the orthorhombic space group P2(1)2(1)2, where a = 105.2 A, b = 182.1 A, and c = 54.5 A. The conformation of the protein around the magnesium pyrophosphate is very similar to that seen when magnesium ADP-beryllium fluoride binds in the active site. The latter complex mimics the binding of ATP prior to hydrolysis. The pyrophosphate molecule occupies the beta- and gamma-phosphate sites, where the two phosphorus atoms are in the same positions as the beta-phosphate and the BeFx moiety of the beryllium fluoride-trapped ADP. The surrounding active site residues are almost perfectly superimposable in the two structures and the hydrogen-bonding interactions that the PPi makes with the protein are essentially identical. The similarity between the MgPPi and MgADP.BeFx complex with S1Dc suggests that the conformational change, which occurs when ATP binds to actomyosin and which reduces the affinity of myosin for actin, is caused by the binding of the gamma- and beta-phosphate groups of the nucleotide. This then implies that the role of the remainder of the substrate is to increase the binding affinity for myosin and thus to drive the equilibrium toward dissociation of myosin from actin.

PubMed: 7619796
DOI: 10.1021/bi00028a005

実験手法

X-RAY DIFFRACTION (2.7 Å)