Structure of human Rad51 protein filament from molecular modeling and site-specific linear dichroism spectroscopy.

ABSTRACT: To get mechanistic insight into the DNA strand-exchange reaction of homologous recombination, we solved a filament structure of a human Rad51 protein, combining molecular modeling with experimental data. We build our structure on reported structures for central and N-terminal parts of pure (uncomplexed) Rad51 protein by aid of linear dichroism spectroscopy, providing angular orientations of substituted tyrosine residues of Rad51-dsDNA filaments in solution. The structure, validated by comparison with an electron microscopy density map and results from mutation analysis, is proposed to represent an active solution structure of the nucleo-protein complex. An inhomogeneously stretched double-stranded DNA fitted into the filament emphasizes the strategic positioning of 2 putative DNA-binding l

SUBMITTER: Reymer A 

PROVIDER: S-EPMC2726390 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature