5BPZ

Atomic-resolution structures of the APC/C subunits Apc4 and the Apc5 N-terminal domain

5BPZ の概要

• エントリーDOI: 10.2210/pdb5bpz/pdb
• 分子名称: Anapc5 protein, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: apc5, apc/c, anaphase promoting complex, cell cycle
• 由来する生物種: Xenopus laevis (African clawed frog)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19577.74

構造登録者

Cronin, N.,Yang, J.,Zhang, Z.,Barford, D. (登録日: 2015-05-28, 公開日: 2015-09-02, 最終更新日: 2024-05-08)

主引用文献

Cronin, N.B.,Yang, J.,Zhang, Z.,Kulkarni, K.,Chang, L.,Yamano, H.,Barford, D.
Atomic-Resolution Structures of the APC/C Subunits Apc4 and the Apc5 N-Terminal Domain.
J.Mol.Biol., 427:3300-3315, 2015

PubMed Abstract: Many essential biological processes are mediated by complex molecular machines comprising multiple subunits. Knowledge on the architecture of individual subunits and their positions within the overall multimeric complex is key to understanding the molecular mechanisms of macromolecular assemblies. The anaphase-promoting complex/cyclosome (APC/C) is a large multisubunit complex that regulates cell cycle progression by ubiquitinating cell cycle proteins for proteolysis by the proteasome. The holo-complex is composed of 15 different proteins that assemble to generate a complex of 20 subunits. Here, we describe the crystal structures of Apc4 and the N-terminal domain of Apc5 (Apc5(N)). Apc4 comprises a WD40 domain split by a long α-helical domain, whereas Apc5(N) has an α-helical fold. In a separate study, we had fitted these atomic models to a 3.6-Å-resolution cryo-electron microscopy map of the APC/C. We describe how, in the context of the APC/C, regions of Apc4 disordered in the crystal assume order through contacts to Apc5, whereas Apc5(N) shows small conformational changes relative to its crystal structure. We discuss the complementary approaches of high-resolution electron microscopy and protein crystallography to the structure determination of subunits of multimeric complexes.

PubMed: 26343760
DOI: 10.1016/j.jmb.2015.08.023

実験手法

X-RAY DIFFRACTION (2.18 Å)