1V5W

Crystal structure of the human Dmc1 protein

1V5W の概要

• エントリーDOI: 10.2210/pdb1v5w/pdb
• 分子名称: Meiotic recombination protein DMC1/LIM15 homolog (2 entities in total)
• 機能のキーワード: dna-binding protein, ring protein, octamer, aaa atpase, riken structural genomics/proteomics initiative, rsgi, structural genomics, recombination
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus (Potential): Q14565
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 76026.61

構造登録者

Kinebuchi, T.,Kagawa, W.,Enomoto, R.,Ikawa, S.,Shibata, T.,Kurumizaka, H.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2003-11-26, 公開日: 2004-05-18, 最終更新日: 2023-10-25)

主引用文献

Kinebuchi, T.,Kagawa, W.,Enomoto, R.,Tanaka, K.,Miyagawa, K.,Shibata, T.,Kurumizaka, H.,Yokoyama, S.
Structural basis for octameric ring formation and DNA interaction of the human homologous-pairing protein dmc1
Mol.Cell, 14:363-374, 2004

PubMed Abstract: The human Dmc1 protein, a RecA/Rad51 homolog, is a meiosis-specific DNA recombinase that catalyzes homologous pairing. RecA and Rad51 form helical filaments, while Dmc1 forms an octameric ring. In the present study, we crystallized the full-length human Dmc1 protein and solved the structure of the Dmc1 octameric ring. The monomeric structure of the Dmc1 protein closely resembled those of the human and archaeal Rad51 proteins. In addition to the polymerization motif that was previously identified in the Rad51 proteins, we found another hydrogen bonding interaction at the polymer interface, which could explain why Dmc1 forms stable octameric rings instead of helical filaments. Mutagenesis studies identified the inner and outer basic patches that are important for homologous pairing. The inner patch binds both single-stranded and double-stranded DNAs, while the outer one binds single-stranded DNA. Based on these results, we propose a model for the interaction of the Dmc1 rings with DNA.

PubMed: 15125839
DOI: 10.1016/S1097-2765(04)00218-7

実験手法

X-RAY DIFFRACTION (3.2 Å)