6BZF

Structure of S. cerevisiae Zip2:Spo16 complex, C2 form

6BZF の概要

• エントリーDOI: 10.2210/pdb6bzf/pdb
• 分子名称: Sporulation-specific protein 16, Protein ZIP2, ... (6 entities in total)
• 機能のキーワード: xpf-ercc1 meiosis recombination, dna binding protein
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 199963.59

構造登録者

Arora, K.,Corbett, K.D. (登録日: 2017-12-23, 公開日: 2018-02-14, 最終更新日: 2023-11-15)

主引用文献

Arora, K.,Corbett, K.D.
The conserved XPF:ERCC1-like Zip2:Spo16 complex controls meiotic crossover formation through structure-specific DNA binding.
Nucleic Acids Res., 47:2365-2376, 2019

PubMed Abstract: In eukaryotic meiosis, generation of haploid gametes depends on the formation of inter-homolog crossovers, which enable the pairing, physical linkage, and eventual segregation of homologs in the meiosis I division. A class of conserved meiosis-specific proteins, collectively termed ZMMs, are required for formation and spatial control of crossovers throughout eukaryotes. Here, we show that three Saccharomyces cerevisiae ZMM proteins-Zip2, Zip4 and Spo16-interact with one another and form a DNA-binding complex critical for crossover formation and control. We determined the crystal structure of a Zip2:Spo16 subcomplex, revealing a heterodimer structurally related to the XPF:ERCC1 endonuclease complex. Zip2:Spo16 lacks an endonuclease active site, but binds specific DNA structures found in early meiotic recombination intermediates. Mutations in multiple DNA-binding surfaces on Zip2:Spo16 severely compromise DNA binding, supporting a model in which the complex's central and HhH domains cooperate to bind DNA. Overall, our data support a model in which the Zip2:Zip4:Spo16 complex binds and stabilizes early meiotic recombination intermediates, then coordinates additional factors to promote crossover formation and license downstream events including synaptonemal complex assembly.

PubMed: 30566683
DOI: 10.1093/nar/gky1273

実験手法

X-RAY DIFFRACTION (2.286 Å)