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1UW0

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

Summary for 1UW0
Entry DOI10.2210/pdb1uw0/pdb
Related1IMO 1IN1
DescriptorDNA LIGASE III, ZINC ION (2 entities in total)
Functional Keywordsdna repair, zinc finger, ligase, parp-like finger, cell division, dna replication, nuclear protein
Biological sourceHOMO SAPIENS (HUMAN)
Cellular locationNucleus: P49916
Total number of polymer chains1
Total formula weight13311.75
Authors
Kulczyk, A.W.,Yang, J.-C.,Neuhaus, D. (deposition date: 2004-01-27, release date: 2004-08-05, Last modification date: 2024-05-15)
Primary citationKulczyk, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

238268

數據於2025-07-02公開中

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