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TitleStructure-function analysis of pneumococcal DprA protein reveals that dimerization is crucial for loading RecA recombinase onto DNA during transformation.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 109, Page E2466-E2475, Year 2012
Publish dateNov 21, 2011 (structure data deposition date)
AuthorsQuevillon-Cheruel, S. / Campo, N. / Mirouze, N. / Mortier-Barriere, I. / Brooks, M.A. / Boudes, M. / Durand, D. / Soulet, A.L. / Lisboa, J. / Noirot, P. ...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.
External linksProc. Natl. Acad. Sci. USA / PubMed:22904190
MethodsX-ray diffraction
Resolution2.7 Å
Structure data

PDB-3uqz:
X-ray structure of DNA processing protein A (DprA) from Streptococcus pneumoniae
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • streptococcus pneumoniae (bacteria)
KeywordsDNA BINDING PROTEIN / SAM and Rossmann Fold / DNA processing protein A

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