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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'''SOLUTION STRUCTURE OF THE ZINC-FINGER DOMAIN FROM DNA LIGASE IIIA'''<br />
'''SOLUTION STRUCTURE OF THE ZINC-FINGER DOMAIN FROM DNA LIGASE IIIA'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1UW0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/DNA_ligase_(ATP) DNA ligase (ATP)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.5.1.1 6.5.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UW0 OCA].
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1UW0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/DNA_ligase_(ATP) DNA ligase (ATP)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.5.1.1 6.5.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UW0 OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Kulczyk, A.W.]]
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[[Category: Kulczyk, A W.]]
[[Category: Neuhaus, D.]]
[[Category: Neuhaus, D.]]
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[[Category: Yang, J.C.]]
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[[Category: Yang, J C.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: cell division]]
[[Category: cell division]]
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[[Category: zinc finger]]
[[Category: zinc finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:39:12 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:28:54 2008''

Revision as of 13:28, 21 February 2008


1uw0

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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 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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