4HYY

Filament of octameric rings of DMC1 recombinase from Homo sapiens

Summary for 4HYY

• Entry DOI: 10.2210/pdb4hyy/pdb
• Related: 1V5W
• Descriptor: Meiotic recombination protein DMC1/LIM15 homolog (2 entities in total)
• Functional Keywords: reca homolog, dna strand exchange, dna, nucleus, recombination
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus (Potential): Q14565
• Total number of polymer chains: 4
• Total formula weight: 118270.04

Authors

Du, L.,Luo, Y. (deposition date: 2012-11-14, release date: 2013-04-10, Last modification date: 2023-09-20)

Primary citation

Du, L.,Luo, Y.
Structure of a filament of stacked octamers of human DMC1 recombinase.
Acta Crystallogr.,Sect.F, 69:382-386, 2013

PubMed 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.

PubMed: 23545642
DOI: 10.1107/S1744309113005678

Experimental method

X-RAY DIFFRACTION (2.603 Å)