4P0S
human Mus81-Eme1-3'flap DNA complex
Summary for 4P0S
| Entry DOI | 10.2210/pdb4p0s/pdb |
| Related | 4P0P 4P0Q 4P0R |
| Descriptor | Crossover junction endonuclease MUS81, Crossover junction endonuclease EME1, DNA GAATGTGTGTCT, ... (5 entities in total) |
| Functional Keywords | resolvase, hydrolase-dna complex, hydrolase/dna |
| Biological source | Homo sapiens (Human) More |
| Cellular location | Nucleus, nucleolus : Q96NY9 Q96AY2 |
| Total number of polymer chains | 20 |
| Total formula weight | 371141.82 |
| Authors | Gwon, G.H.,Baek, K.,Cho, Y. (deposition date: 2014-02-22, release date: 2014-05-28, Last modification date: 2023-12-27) |
| Primary citation | Gwon, G.H.,Jo, A.,Baek, K.,Jin, K.S.,Fu, Y.,Lee, J.B.,Kim, Y.,Cho, Y. Crystal structures of the structure-selective nuclease Mus81-Eme1 bound to flap DNA substrates. Embo J., 33:1061-1072, 2014 Cited by PubMed Abstract: The Mus81-Eme1 complex is a structure-selective endonuclease with a critical role in the resolution of recombination intermediates during DNA repair after interstrand cross-links, replication fork collapse, or double-strand breaks. To explain the molecular basis of 3' flap substrate recognition and cleavage mechanism by Mus81-Eme1, we determined crystal structures of human Mus81-Eme1 bound to various flap DNA substrates. Mus81-Eme1 undergoes gross substrate-induced conformational changes that reveal two key features: (i) a hydrophobic wedge of Mus81 that separates pre- and post-nick duplex DNA and (ii) a "5' end binding pocket" that hosts the 5' nicked end of post-nick DNA. These features are crucial for comprehensive protein-DNA interaction, sharp bending of the 3' flap DNA substrate, and incision strand placement at the active site. While Mus81-Eme1 unexpectedly shares several common features with members of the 5' flap nuclease family, the combined structural, biochemical, and biophysical analyses explain why Mus81-Eme1 preferentially cleaves 3' flap DNA substrates with 5' nicked ends. PubMed: 24733841DOI: 10.1002/embj.201487820 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (6 Å) |
Structure validation
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