1XNA

NMR SOLUTION STRUCTURE OF THE SINGLE-STRAND BREAK REPAIR PROTEIN XRCC1-N-TERMINAL DOMAIN

Summary for 1XNA

• Entry DOI: 10.2210/pdb1xna/pdb
• Descriptor: PROTEIN (DNA-REPAIR PROTEIN XRCC1) (1 entity in total)
• Functional Keywords: xrcc1, 3d nmr, dna repair, single-strand break dna binding, dna polymerase-beta binding, beta sandwich, dna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P18887
• Total number of polymer chains: 1
• Total formula weight: 20245.67

Authors

Marintchev, A.,Mullen, G.P. (deposition date: 1999-02-27, release date: 1999-09-01, Last modification date: 2023-12-27)

Primary citation

Marintchev, A.,Mullen, M.A.,Maciejewski, M.W.,Pan, B.,Gryk, M.R.,Mullen, G.P.
Solution structure of the single-strand break repair protein XRCC1 N-terminal domain.
Nat.Struct.Biol., 6:884-893, 1999

PubMed Abstract: XRCC1 functions in the repair of single-strand DNA breaks in mammalian cells and forms a repair complex with beta-Pol, ligase III and PARP. Here we describe the NMR solution structure of the XRCC1 N-terminal domain (XRCC1 NTD). The structural core is a beta-sandwich with beta-strands connected by loops, three helices and two short two-stranded beta-sheets at each connection side. We show, for the first time, that the XRCC1 NTD specifically binds single-strand break DNA (gapped and nicked). We also show that the XRCC1 NTD binds a gapped DNA-beta-Pol complex. The DNA binding and beta-Pol binding surfaces were mapped by NMR and found to be well suited for interaction with single-strand gap DNA containing a 90 degrees bend, and for simultaneously making contacts with the palm-thumb of beta-Pol in a ternary complex. The findings suggest a mechanism for preferential binding of the XRCC1 NTD to flexible single-strand break DNA.

PubMed: 10467102
DOI: 10.1038/12347

Experimental method

SOLUTION NMR