4HYY: Filament Of Octameric Rings Of Dmc1 Recombinase From Homo Sapiens

Citation:
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. (2013) 69 p.382-386
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.
PDB ID: 4HYYDownload
MMDB ID: 109039
PDB Deposition Date: 2012/11/14
Updated in MMDB: 2013/04
Experimental Method:
x-ray diffraction
Resolution: 2.6  Å
Source Organism:
Similar Structures:
Biological Unit for 4HYY: octameric; determined by author and by software (PISA)
Molecular Components in 4HYY
Label Count Molecule
Proteins (8 molecules)
8
Meiotic Recombination Protein Dmc1/lim15 Homolog(Gene symbol: DMC1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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