3IF8

Crystal Structure of ZWILCH, a member of the RZZ kinetochore complex

3IF8 の概要

• エントリーDOI: 10.2210/pdb3if8/pdb
• 分子名称: Protein zwilch homolog (3 entities in total)
• 機能のキーワード: incomplete beta-barrel, alternative splicing, cell cycle, cell division, kinetochore, mitosis, polymorphism
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Chromosome, centromere, kinetochore: Q9H900 Q9H900
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67723.39

構造登録者

Wehenkel, A.,Civril, F.,Musacchio, A. (登録日: 2009-07-24, 公開日: 2010-06-09, 最終更新日: 2024-03-20)

主引用文献

Civril, F.,Wehenkel, A.,Giorgi, F.M.,Santaguida, S.,Di Fonzo, A.,Grigorean, G.,Ciccarelli, F.D.,Musacchio, A.
Structural analysis of the RZZ complex reveals common ancestry with multisubunit vesicle tethering machinery.
Structure, 18:616-626, 2010

PubMed Abstract: The RZZ complex recruits dynein to kinetochores. We investigated structure, topology, and interactions of the RZZ subunits (ROD, ZWILCH, and ZW10) in vitro, in vivo, and in silico. We identify neuroblastoma-amplified gene (NAG), a ZW10 binder, as a ROD homolog. ROD and NAG contain an N-terminal beta propeller followed by an alpha solenoid, which is the architecture of certain nucleoporins and vesicle coat subunits, suggesting a distant evolutionary relationship. ZW10 binding to ROD and NAG is mutually exclusive. The resulting ZW10 complexes (RZZ and NRZ) respectively contain ZWILCH and RINT1 as additional subunits. The X-ray structure of ZWILCH, the first for an RZZ subunit, reveals a novel fold distinct from RINT1's. The evolutionarily conserved NRZ likely acts as a tethering complex for retrograde trafficking of COPI vesicles from the Golgi to the endoplasmic reticulum. The RZZ, limited to metazoans, probably evolved from the NRZ, exploiting the dynein-binding capacity of ZW10 to direct dynein to kinetochores.

PubMed: 20462495
DOI: 10.1016/j.str.2010.02.014

実験手法

X-RAY DIFFRACTION (2.55 Å)