4Y66

Crystal structure of Giardia lamblia Hop2-Mnd1 complex

Summary for 4Y66

• Entry DOI: 10.2210/pdb4y66/pdb
• Descriptor: Mnd1, Putative tbpip family protein (2 entities in total)
• Functional Keywords: cell cycle
• Biological source: Giardia lamblia ATCC 50803; More
• Total number of polymer chains: 6
• Total formula weight: 147153.57

Authors

Kang, H.A.,Shin, H.C.,Oh, B.H. (deposition date: 2015-02-12, release date: 2015-03-18, Last modification date: 2024-03-20)

Primary citation

Kang, H.A.,Shin, H.C.,Kalantzi, A.S.,Toseland, C.P.,Kim, H.M.,Gruber, S.,Peraro, M.D.,Oh, B.H.
Crystal structure of Hop2-Mnd1 and mechanistic insights into its role in meiotic recombination
Nucleic Acids Res., 43:3841-3856, 2015

PubMed Abstract: In meiotic DNA recombination, the Hop2-Mnd1 complex promotes Dmc1-mediated single-stranded DNA (ssDNA) invasion into homologous chromosomes to form a synaptic complex by a yet-unclear mechanism. Here, the crystal structure of Hop2-Mnd1 reveals that it forms a curved rod-like structure consisting of three leucine zippers and two kinked junctions. One end of the rod is linked to two juxtaposed winged-helix domains, and the other end is capped by extra α-helices to form a helical bundle-like structure. Deletion analysis shows that the helical bundle-like structure is sufficient for interacting with the Dmc1-ssDNA nucleofilament, and molecular modeling suggests that the curved rod could be accommodated into the helical groove of the nucleofilament. Remarkably, the winged-helix domains are juxtaposed at fixed relative orientation, and their binding to DNA is likely to perturb the base pairing according to molecular simulations. These findings allow us to propose a model explaining how Hop2-Mnd1 juxtaposes Dmc1-bound ssDNA with distorted recipient double-stranded DNA and thus facilitates strand invasion.

PubMed: 25740648
DOI: 10.1093/nar/gkv172

Experimental method

X-RAY DIFFRACTION (3.2 Å)