1IJJ
THE X-RAY CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN RABBIT SKELETAL MUSCLE ACTIN AND LATRUNCULIN A AT 2.85 A RESOLUTION
1IJJ の概要
エントリーDOI | 10.2210/pdb1ijj/pdb |
関連するPDBエントリー | 1ATN 1ESV |
分子名称 | ACTIN, ALPHA SKELETAL MUSCLE, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total) |
機能のキーワード | actin, latrunculin, cytoskeleton, contractile protein |
由来する生物種 | Oryctolagus cuniculus (rabbit) |
細胞内の位置 | Cytoplasm, cytoskeleton: P68135 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 86099.98 |
構造登録者 | |
主引用文献 | Bubb, M.R.,Govindasamy, L.,Yarmola, E.G.,Vorobiev, S.M.,Almo, S.C.,Somasundaram, T.,Chapman, M.S.,Agbandje-McKenna, M.,McKenna, R. Polylysine induces an antiparallel actin dimer that nucleates filament assembly: crystal structure at 3.5-A resolution J.Biol.Chem., 277:20999-21006, 2002 Cited by PubMed Abstract: An antiparallel actin dimer has been proposed to be an intermediate species during actin filament nucleation. We now show that latrunculin A, a marine natural product that inhibits actin polymerization, arrests polylysine-induced nucleation at the level of an antiparallel dimer, resulting in its accumulation. These dimers, when composed of pyrene-labeled actin subunits, give rise to a fluorescent excimer, permitting detection during polymerization in vitro. We report the crystallographic structure of the polylysine-actin-latrunculin A complex at 3.5-A resolution. The non-crystallographic contact is consistent with a dimeric structure and confirms the antiparallel orientation of its subunits. The crystallographic contacts reveal that the mobile DNase I binding loop of one subunit of a symmetry-related antiparallel actin dimer is partially stabilized in the interface between the two subunits of a second antiparallel dimer. These results provide a potential explanation for the paradoxical nucleation of actin filaments that have exclusively parallel subunits by a dimer containing antiparallel subunits. PubMed: 11932258DOI: 10.1074/jbc.M201371200 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.85 Å) |
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