Three‐dimensional architecture of the eukaryotic multisynthetase complex determined from negatively stained and cryoelectron micrographs

FEBS Letters

Norcum, Mona T²  Boisset, Nicolas¹ 

[1] Laboratoire de Minéralogie Cristallographie, Universités Paris 6 et Paris 7, Paris Cedex 05, France;Department of Biochemistry, The University of Mississippi Medical Center, 2500 North State Street, Jackson, MS 39216, USA

关键词: Aminoacyl-tRNA synthetase;    Multisynthetase complex;    Electron microscopy;    Three-dimensional reconstruction;   

DOI  :  10.1016/S0014-5793(02)02262-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

This study provides the first description of the three-dimensional architecture of the multienzyme complex of aminoacyl-tRNA synthetases. Reconstructions were calculated from electron microscopic images of negatively stained and frozen hydrated samples using three independent angular assignment methods. In all cases, volumes show an asymmetric triangular arrangement of protein domains around a deep central cavity. The structures have openings or indentations on most sides. Maximum dimensions are ca. 19×16×10 nm. The central cavity is 4 nm in diameter and extends two-thirds of the length of the particle.

【 授权许可】

Unknown