6BZF

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

Summary for 6BZF

• Entry DOI: 10.2210/pdb6bzf/pdb
• Descriptor: Sporulation-specific protein 16, Protein ZIP2, ... (6 entities in total)
• Functional Keywords: xpf-ercc1 meiosis recombination, dna binding protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 8
• Total formula weight: 199963.59

Authors

Arora, K.,Corbett, K.D. (deposition date: 2017-12-23, release date: 2018-02-14, Last modification date: 2023-11-15)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.286 Å)