1BR4

SMOOTH MUSCLE MYOSIN MOTOR DOMAIN-ESSENTIAL LIGHT CHAIN COMPLEX WITH MGADP.BEF3 BOUND AT THE ACTIVE SITE

1BR4 の概要

• エントリーDOI: 10.2210/pdb1br4/pdb
• 分子名称: MYOSIN, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: muscle protein
• 由来する生物種: Gallus gallus (chicken); 詳細
• 細胞内の位置: Cytoplasm, myofibril: P10587
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 444350.87

構造登録者

Dominguez, R.,Trybus, K.M.,Cohen, C. (登録日: 1998-08-27, 公開日: 1998-09-09, 最終更新日: 2024-04-03)

主引用文献

Dominguez, R.,Freyzon, Y.,Trybus, K.M.,Cohen, C.
Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state.
Cell(Cambridge,Mass.), 94:559-571, 1998

PubMed Abstract: The crystal structures of an expressed vertebrate smooth muscle myosin motor domain (MD) and a motor domain-essential light chain (ELC) complex (MDE), both with a transition state analog (MgADP x AIF4-) in the active site, have been determined to 2.9 A and 3.5 A resolution, respectively. The MDE structure with an ATP analog (MgADP x BeFx) was also determined to 3.6 A resolution. In all three structures, a domain of the C-terminal region, the "converter," is rotated approximately 70 degrees from that in nucleotide-free skeletal subfragment 1 (S1). We have found that the MDE-BeFx and MDE-AIF4- structures are almost identical, consistent with the fact that they both bind weakly to actin. A comparison of the lever arm positions in MDE-AIF4- and in nucleotide-free skeletal S1 shows that a potential displacement of approximately 10 nm can be achieved during the power stroke.

PubMed: 9741621
DOI: 10.1016/S0092-8674(00)81598-6

実験手法

X-RAY DIFFRACTION (3.62 Å)