XPA, a 273 amino acid protein, is involved in the early stage of the nucleotide excision repair process, by which a variety of DNA lesions are removed from the genome. NMR was used to analyze the structure of the central domain of XPA, which encompasses residues 98 to 219, and contains a zinc coordinating motif. Following chemical shift assignments of the backbone and side-chain 1H, 15N, and 13C nuclei, the tertiary structure was determined by multi-dimensional and multi-resonance NMR methods. The structure shows that the central domain consists of two subdomains, a zinc-containing subdomain and a C-terminal subdomain, which are connected by a short linker sequence. The fold adopted by the zinc-containing subdomain is similar to those of zinc fingers in transcription factors, which bind to DNA in a sequence specific manner. In contrast to these zinc fingers, the zinc-containing subdomain of XPA is dominantly negatively charged, and thus unlikely to directly bind to DNA. The interaction of the central domain of XPA with a damaged DNA was investigated by a chemical shift perturbation experiment, which suggests that the DNA interact with the positively charged cleft in the C-terminal subdomain, and not with the zinc-containing subdomain. The backbone dynamics were analyzed with 15N longitudinal (T 1), transverse (T 2), and NOE (nuclear Overhauser effect) relaxation data. The results show that the proposed DNA-binding surface exhibits a highly dynamical feature, which may be necessary for interacting structurally with various DNA damages.