1UW0

Solution structure of the zinc-finger domain from DNA ligase IIIa

1UW0 の概要

• エントリーDOI: 10.2210/pdb1uw0/pdb
• 関連するPDBエントリー: 1IMO 1IN1
• 分子名称: DNA LIGASE III, ZINC ION (2 entities in total)
• 機能のキーワード: dna repair, zinc finger, ligase, parp-like finger, cell division, dna replication, nuclear protein
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Nucleus: P49916
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13311.75

構造登録者

Kulczyk, A.W.,Yang, J.-C.,Neuhaus, D. (登録日: 2004-01-27, 公開日: 2004-08-05, 最終更新日: 2024-05-15)

主引用文献

Kulczyk, A.W.,Yang, J.-C.,Neuhaus, D.
Solution Structure and DNA Binding of the Zinc-Finger Domain from DNA Ligase Iiialpha
J.Mol.Biol., 341:723-, 2004

PubMed Abstract: DNA ligase IIIalpha carries out the final ligation step in the base excision repair (BER) and single strand break repair (SSBR) mechanisms of DNA repair. The enzyme recognises single-strand nicks and other damage features in double-stranded DNA, both through the catalytic domain and an N-terminal domain containing a single zinc finger. The latter is homologous to other zinc fingers that recognise damaged DNA, two in the N terminus of poly(adenosine-ribose)polymerase and three in the N terminus of the Arabidopsis thaliana nick-sensing DNA 3'-phosphoesterase. Here, we present the solution structure of the zinc-finger domain of human DNA ligase IIIalpha, the first structure of a finger from this group. It is related to that of the erythroid transcription factor GATA-1, but has an additional N-terminal beta-strand and C-terminal alpha-helix. Chemical shift mapping using a DNA ligand containing a single-stranded break showed that the DNA-binding surface of the DNA-ligase IIIalpha zinc finger is substantially different from that of GATA-1, consistent with the fact that the two proteins recognise very different features in the DNA. Likely implications for DNA binding are discussed.

PubMed: 15288782
DOI: 10.1016/J.JMB.2004.06.035

実験手法

SOLUTION NMR