1uw0
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(New page: 200px<br /> <applet load="1uw0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uw0" /> '''SOLUTION STRUCTURE OF THE ZINC-FINGER DOMAI...)
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Revision as of 17:32, 12 November 2007
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SOLUTION STRUCTURE OF THE ZINC-FINGER DOMAIN FROM DNA LIGASE IIIA
Overview
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.
About this Structure
1UW0 is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Active as DNA ligase (ATP), with EC number 6.5.1.1 Full crystallographic information is available from OCA.
Reference
Solution structure and DNA binding of the zinc-finger domain from DNA ligase IIIalpha., Kulczyk AW, Yang JC, Neuhaus D, J Mol Biol. 2004 Aug 13;341(3):723-38. PMID:15288782
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