1HLU
STRUCTURE OF BOVINE BETA-ACTIN-PROFILIN COMPLEX WITH ACTIN BOUND ATP PHOSPHATES SOLVENT ACCESSIBLE
1HLU の概要
| エントリーDOI | 10.2210/pdb1hlu/pdb |
| 分子名称 | BETA-ACTIN, PROFILIN, CALCIUM ION, ... (4 entities in total) |
| 機能のキーワード | complex (acetylation-actin-binding), actin, profilin, conformational changes, cytoskeleton, complex (acetylation-actin-binding) complex, complex (acetylation/actin-binding) |
| 由来する生物種 | Bos taurus (cattle) 詳細 |
| 細胞内の位置 | Cytoplasm, cytoskeleton: P60712 P02584 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 57205.96 |
| 構造登録者 | |
| 主引用文献 | Chik, J.K.,Lindberg, U.,Schutt, C.E. The structure of an open state of beta-actin at 2.65 A resolution. J.Mol.Biol., 263:607-623, 1996 Cited by PubMed Abstract: The structure of an "open state" of crystalline profilin:beta-actin has been solved to 2.65 A by X-ray crystallography. The open-state crystals, in 1.8 M potassium phosphate, have an expanded unit cell dimension in the c direction of 185.7 A compared with 171.9 A in the previously solved ammonium sulphate-stabilized "tight-state" structure. The unit cell change between the open and the tight states is accompanied by large subdomain movements in actin. Furthermore, the nucleotide in the open state is significantly more exposed to solvent, and local conformational changes in the hydrophobic pocket surrounding cysteine 374 occur during the transition to the tight state. Significant changes were observed at the N terminus and in the DNase-I binding loop. Neither the structure of profilin nor its contact with beta-actin are affected by the changes in the unit cell. Applying osmotic pressure to profilin:beta-actin crystals brings about a collapse of the unit cell comparable with that seen in the open to tight-state transition, enabling an estimate of the work required to cause this transformation of beta-actin in the crystals. The slight difference in energy between the open and collapsed states explains the extreme sensitivity of profilin:beta-actin crystals to changes in chemical and thermal environment. PubMed: 8918942DOI: 10.1006/jmbi.1996.0602 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.65 Å) |
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