1EW1

RECA PROTEIN-BOUND SINGLE-STRANDED DNA

Summary for 1EW1

• Entry DOI: 10.2210/pdb1ew1/pdb
• Related: 3rec
• Descriptor: DNA (5'-D(*TP*AP*CP*G)-3') (1 entity in total)
• Functional Keywords: deoxyribose-base stacking, single-stranded dna, dna
• Total number of polymer chains: 1
• Total formula weight: 1190.83

Authors

Nishinaka, T.,Ito, Y.,Yokoyama, S.,Shibata, T. (deposition date: 2000-04-21, release date: 2000-05-08, Last modification date: 2024-05-22)

Primary citation

Nishinaka, T.,Ito, Y.,Yokoyama, S.,Shibata, T.
An extended DNA structure through deoxyribose-base stacking induced by RecA protein.
Proc.Natl.Acad.Sci.USA, 94:6623-6628, 1997

PubMed Abstract: The family of proteins that are homologous to RecA protein of Escherichia coli is essential to homologous genetic recombination in various organisms including viruses, bacteria, lower eukaryotes, and mammals. In the presence of ATP (or ATPgammaS), these proteins form helical filaments containing single-stranded DNA at the center. The single-stranded DNA bound to RecA protein is extended 1.5 times relative to B-form DNA with the same sequence, and the extension is critical to pairing with homologous double-stranded DNA. This pairing reaction, called homologous pairing, is a key reaction in homologous recombination. In this NMR study, we determined a three-dimensional structure of the single-stranded DNA bound to RecA protein. The DNA structure contains novel deoxyribose-base stacking in which the 2'-methylene moiety of each deoxyribose is placed above the base of the following residue, instead of normal stacking of adjacent bases. As a result of this deoxyribose-base stacking, bases of the single-stranded DNA are spaced out nearly 5 A. Thus, this novel structure well explains the axial extension of DNA in the RecA-filaments relative to B-form DNA and leads to a possible interpretation of the role of this extension in homologous pairing.

PubMed: 9192615
DOI: 10.1073/pnas.94.13.6623

Experimental method

SOLUTION NMR