1s10
From Proteopedia
(New page: 200px<br /><applet load="1s10" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s10, resolution 2.1Å" /> '''Snapshots of replicat...) |
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| - | [[Image:1s10.gif|left|200px]]<br /><applet load="1s10" size=" | + | [[Image:1s10.gif|left|200px]]<br /><applet load="1s10" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1s10, resolution 2.1Å" /> | caption="1s10, resolution 2.1Å" /> | ||
'''Snapshots of replication through an abasic lesion: structural basis for base substitution and frameshift'''<br /> | '''Snapshots of replication through an abasic lesion: structural basis for base substitution and frameshift'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Dpo4 from S. Solfataricus, a DinB-like Y family polymerase, efficiently | + | Dpo4 from S. Solfataricus, a DinB-like Y family polymerase, efficiently replicates DNA past an abasic lesion. We have determined crystal structures of Dpo4 complexed with five different abasic site-containing DNA substrates and find that translesion synthesis is template directed with the abasic site looped out and the incoming nucleotide is opposite the base 5' to the lesion. The ensuing DNA synthesis generates a -1 frameshift when the abasic site remains extrahelical. Template realignment during primer extension is also observed, resulting in base substitutions or even +1 frameshifts. In the case of a +1 frameshift, the extra nucleotide is accommodated in the solvent-exposed minor groove. In addition, the structure of an unproductive Dpo4 ternary complex suggests that the flexible little finger domain facilitates DNA orientation and translocation during translesion synthesis. |
==About this Structure== | ==About this Structure== | ||
| - | 1S10 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with CA and DCP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] Full crystallographic information is available from [http:// | + | 1S10 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=DCP:'>DCP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S10 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: polymerase]] | [[Category: polymerase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:56:44 2008'' |
Revision as of 12:56, 21 February 2008
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Snapshots of replication through an abasic lesion: structural basis for base substitution and frameshift
Overview
Dpo4 from S. Solfataricus, a DinB-like Y family polymerase, efficiently replicates DNA past an abasic lesion. We have determined crystal structures of Dpo4 complexed with five different abasic site-containing DNA substrates and find that translesion synthesis is template directed with the abasic site looped out and the incoming nucleotide is opposite the base 5' to the lesion. The ensuing DNA synthesis generates a -1 frameshift when the abasic site remains extrahelical. Template realignment during primer extension is also observed, resulting in base substitutions or even +1 frameshifts. In the case of a +1 frameshift, the extra nucleotide is accommodated in the solvent-exposed minor groove. In addition, the structure of an unproductive Dpo4 ternary complex suggests that the flexible little finger domain facilitates DNA orientation and translocation during translesion synthesis.
About this Structure
1S10 is a Single protein structure of sequence from Sulfolobus solfataricus with and as ligands. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.
Reference
Snapshots of replication through an abasic lesion; structural basis for base substitutions and frameshifts., Ling H, Boudsocq F, Woodgate R, Yang W, Mol Cell. 2004 Mar 12;13(5):751-62. PMID:15023344
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