PDBsum entry 4hyy

Recombination

PDB id: 4hyy

Contents

Protein chain

241 a.a.

Waters ×96

PDB id:

4hyy

Name:

Recombination

Title:

Filament of octameric rings of dmc1 recombinase from homo sapiens

Structure:

Meiotic recombination protein dmc1/lim15 homolog. Chain: a, b, c, d. Fragment: atpase domain. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: dmc1, dmc1h, lim15. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.60Å R-factor: 0.182 R-free: 0.246

Authors:

L.Du,Y.Luo

Key ref:

L.Du and Y.Luo (2013). Structure of a filament of stacked octamers of human DMC1 recombinase. Acta Crystallogr Sect F Struct Biol Cryst Commun, 69, 382-386. PubMed id: 23545642 DOI: 10.1107/S1744309113005678

Date:

14-Nov-12 Release date: 10-Apr-13

Protein chains

Q14565  (DMC1_HUMAN) -  Meiotic recombination protein DMC1/LIM15 homolog from Homo sapiens

Seq: 340 a.a.

Struc: 241 a.a.

DOI no: 10.1107/S1744309113005678

Acta Crystallogr Sect F Struct Biol Cryst Commun 69:382-386 (2013)

PubMed id: 23545642

Structure of a filament of stacked octamers of human DMC1 recombinase.

L.Du, Y.Luo.

ABSTRACT

Eukaryal DMC1 proteins play a central role in homologous recombination in meiosis by assembling at the sites of programmed DNA double-strand breaks and carrying out a search for allelic DNA sequences located on homologous chromatids. They are close homologs of eukaryal Rad51 and archaeal RadA proteins and are remote homologs of bacterial RecA proteins. These recombinases (also called DNA strand-exchange proteins) promote a pivotal strand-exchange reaction between homologous single-stranded and double-stranded DNA substrates. An octameric form of a truncated human DMC1 devoid of its small N-terminal domain (residues 1-83) has been crystallized. The structure of the truncated DMC1 octamer is similar to that of the previously reported full-length DMC1 octamer, which has disordered N-terminal domains. In each protomer, only the ATP cap regions (Asp317-Glu323) show a noticeable conformational difference. The truncated DMC1 octamers further stack with alternate polarity into a filament. Similar filamentous assemblies of DMC1 have been observed to form on DNA by electron microscopy.