3UQZ

X-ray structure of DNA processing protein A (DprA) from Streptococcus pneumoniae

Summary for 3UQZ

• Entry DOI: 10.2210/pdb3uqz/pdb
• Descriptor: DNA processing protein DprA, SULFATE ION (3 entities in total)
• Functional Keywords: sam and rossmann fold, dna processing protein a, dna binding protein
• Biological source: Streptococcus pneumoniae
• Total number of polymer chains: 3
• Total formula weight: 96870.31

Authors

Quevillon-Cheruel, S.,Brooks, M.A.,Li de la Sierra-Gallay, I. (deposition date: 2011-11-21, release date: 2012-08-29, Last modification date: 2024-11-20)

Primary citation

Quevillon-Cheruel, S.,Campo, N.,Mirouze, N.,Mortier-Barriere, I.,Brooks, M.A.,Boudes, M.,Durand, D.,Soulet, A.L.,Lisboa, J.,Noirot, P.,Martin, B.,van Tilbeurgh, H.,Noirot-Gros, M.F.,Claverys, J.P.,Polard, P.
Structure-function analysis of pneumococcal DprA protein reveals that dimerization is crucial for loading RecA recombinase onto DNA during transformation.
Proc.Natl.Acad.Sci.USA, 109:E2466-E2475, 2012

PubMed Abstract: Transformation promotes genome plasticity in bacteria via RecA-driven homologous recombination. In the gram-positive human pathogen Streptococcus pneumoniae, the transformasome a multiprotein complex, internalizes, protects, and processes transforming DNA to generate chromosomal recombinants. Double-stranded DNA is internalized as single strands, onto which the transformation-dedicated DNA processing protein A (DprA) ensures the loading of RecA to form presynaptic filaments. We report that the structure of DprA consists of the association of a sterile alpha motif domain and a Rossmann fold and that DprA forms tail-to-tail dimers. The isolation of DprA self-interaction mutants revealed that dimerization is crucial for the formation of nucleocomplexes in vitro and for genetic transformation. Residues important for DprA-RecA interaction also were identified and mutated, establishing this interaction as equally important for transformation. Positioning of key interaction residues on the DprA structure revealed an overlap of DprA-DprA and DprA-RecA interaction surfaces. We propose a model in which RecA interaction promotes rearrangement or disruption of the DprA dimer, enabling the subsequent nucleation of RecA and its polymerization onto ssDNA.

PubMed: 22904190
DOI: 10.1073/pnas.1205638109

Experimental method

X-RAY DIFFRACTION (2.7 Å)