1D1C

DICTYOSTELIUM MYOSIN S1DC (MOTOR DOMAIN FRAGMENT) COMPLEXED WITH N-METHYL-O-NITROPHENYL AMINOETHYLDIPHOSPHATE BERYLLIUM TRIFLUORIDE.

1D1C の概要

• エントリーDOI: 10.2210/pdb1d1c/pdb
• 関連するPDBエントリー: 1D0X 1D0Y 1D0Z 1D1A 1D1B 1D1C
• 分子名称: MYOSIN, MAGNESIUM ION, N-METHYL O-NITROPHENYL AMINOETHYLDIPHOSPHATE BERYLLIUM TRIFLUORIDE, ... (4 entities in total)
• 機能のキーワード: myosin, motility, actin-binding, motor domain, nanologs, 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: 87180.58

構造登録者

Gulick, A.M.,Bauer, C.B.,Thoden, J.B.,Pate, E.,Yount, R.G.,Rayment, I. (登録日: 1999-09-15, 公開日: 2000-01-12, 最終更新日: 2024-02-07)

主引用文献

Gulick, A.M.,Bauer, C.B.,Thoden, J.B.,Pate, E.,Yount, R.G.,Rayment, I.
X-ray structures of the Dictyostelium discoideum myosin motor domain with six non-nucleotide analogs.
J.Biol.Chem., 275:398-408, 2000

PubMed Abstract: The three-dimensional structures of the truncated myosin head from Dictyostelium discoideum myosin II complexed with dinitrophenylaminoethyl-, dinitrophenylaminopropyl-, o-nitrophenylaminoethyl-, m-nitrophenylaminoethyl-, p-nitrophenylaminoethyl-, and o-nitrophenyl-N-methyl-aminoethyl-diphosphate.beryllium fluoride have been determined to better than 2.3-A resolution. The structure of the protein and nucleotide binding pocket in these complexes is very similar to that of S1dC.ADP.BeF(x) (Fisher, A. J., Smith, C. A., Thoden, J., Smith, R., Sutoh, K., Holden, H. M., and Rayment, I. (1995) Biochemistry 34, 8960-8972). The position of the triphosphate-like moiety is essentially identical in all complexes. Furthermore, the alkyl-amino group plays the same role as the ribose by linking the triphosphate to the adenine binding pocket; however, none of the phenyl groups lie in the same position as adenine in S1dC.MgADP.BeF(x), even though several of these nucleotide analogs are functionally equivalent to ATP. Rather the former location of adenine is occupied by water in the nanolog complexes, and the phenyl groups are organized in a manner that attempts to optimize their hydrogen bonding interactions with this constellation of solvent molecules. A comparison of the kinetic and structural properties of the nanologs relative to ATP suggests that the ability of a substrate to sustain tension and to generate movement correlates with a well defined interaction with the active site water structure observed in S1dC.MgADP.BeF(x).

PubMed: 10617631
DOI: 10.1074/jbc.275.1.398

実験手法

X-RAY DIFFRACTION (2.3 Å)