PDBsum entry 2ziu

Hydrolase

PDB id: 2ziu

Contents

Protein chains

281 a.a. *

258 a.a. *

Waters ×56

* Residue conservation analysis

PDB id:

2ziu

Name:

Hydrolase

Title:

Crystal structure of the mus81-eme1 complex

Structure:

Mus81 protein. Chain: a. Fragment: nuclease domain and c-terminal domain, unp residues 303- 612. Synonym: DNA structure specific endonuclease mus81. Engineered: yes. Crossover junction endonuclease eme1. Chain: b. Fragment: nuclease-like domain and c-terminal domain, unp residues

Source:

Danio rerio. Zebrafish. Organism_taxid: 7955. Gene: mus81. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Homo sapiens. Human. Organism_taxid: 9606.

Resolution:

2.70Å R-factor: 0.234 R-free: 0.286

Authors:

J.H.Chang,J.J.Kim,J.M.Choi,J.H.Lee,Y.Cho

Key ref:

J.H.Chang et al. (2008). Crystal structure of the Mus81-Eme1 complex. Genes Dev, 22, 1093-1106. PubMed id: 18413719

Date:

25-Feb-08 Release date: 29-Apr-08

Protein chain

Q7SXA9  (MUS81_DANRE) -  Crossover junction endonuclease MUS81 from Danio rerio

Seq: 604 a.a.

Struc: 281 a.a.*

Protein chain

Q96AY2  (EME1_HUMAN) -  Crossover junction endonuclease EME1 from Homo sapiens

Seq: 570 a.a.

Struc: 258 a.a.

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, B: E.C.3.1.22.- - ?????

Genes Dev 22:1093-1106 (2008)

PubMed id: 18413719

Crystal structure of the Mus81-Eme1 complex.

J.H.Chang, J.J.Kim, J.M.Choi, J.H.Lee, Y.Cho.

ABSTRACT

The Mus81-Eme1 complex is a structure-specific endonuclease that plays an important role in rescuing stalled replication forks and resolving the meiotic recombination intermediates in eukaryotes. We have determined the crystal structure of the Mus81-Eme1 complex. Both Mus81 and Eme1 consist of a central nuclease domain, two repeats of the helix-hairpin-helix (HhH) motif at their C-terminal region, and a linker helix. While each domain structure resembles archaeal XPF homologs, the overall structure is significantly different from those due to the structure of a linker helix. We show that a flexible intradomain linker that formed with 36 residues in the nuclease domain of Eme1 is essential for the recognition of DNA. We identified several basic residues lining the outer surface of the active site cleft of Mus81 that are involved in the interaction with a flexible arm of a nicked Holliday junction (HJ). These interactions might contribute to the optimal positioning of the opposite junction across the nick into the catalytic site, which provided the basis for the "nick and counternick" mechanism of Mus81-Eme1 and for the nicked HJ to be the favored in vitro substrate of this enzyme.