1n48
From Proteopedia
(New page: 200px<br /><applet load="1n48" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n48, resolution 2.2Å" /> '''Y-family DNA polymera...) |
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| - | [[Image:1n48.gif|left|200px]]<br /><applet load="1n48" size=" | + | [[Image:1n48.gif|left|200px]]<br /><applet load="1n48" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1n48, resolution 2.2Å" /> | caption="1n48, resolution 2.2Å" /> | ||
'''Y-family DNA polymerase Dpo4 in complex with DNA containing abasic lesion'''<br /> | '''Y-family DNA polymerase Dpo4 in complex with DNA containing abasic lesion'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4) is a DinB homolog that | + | Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4) is a DinB homolog that belongs to the recently described Y-family of DNA polymerases, which are best characterized by their low-fidelity synthesis on undamaged DNA templates and propensity to traverse normally replication-blocking lesions. Crystal structures of Dpo4 in ternary complexes with DNA and an incoming nucleotide, either correct or incorrect, have been solved at 1.7 A and 2.1 A resolution, respectively. Despite a conserved active site and a hand-like configuration similar to all known polymerases, Dpo4 makes limited and nonspecific contacts with the replicating base pair, thus relaxing base selection. Dpo4 is also captured in the crystal translocating two template bases to the active site at once, suggesting a possible mechanism for bypassing thymine dimers. |
==About this Structure== | ==About this Structure== | ||
| - | 1N48 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 ATP 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:// | + | 1N48 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=ATP:'>ATP</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=1N48 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: y-family]] | [[Category: y-family]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:05 2008'' |
Revision as of 12:02, 21 February 2008
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Y-family DNA polymerase Dpo4 in complex with DNA containing abasic lesion
Overview
Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4) is a DinB homolog that belongs to the recently described Y-family of DNA polymerases, which are best characterized by their low-fidelity synthesis on undamaged DNA templates and propensity to traverse normally replication-blocking lesions. Crystal structures of Dpo4 in ternary complexes with DNA and an incoming nucleotide, either correct or incorrect, have been solved at 1.7 A and 2.1 A resolution, respectively. Despite a conserved active site and a hand-like configuration similar to all known polymerases, Dpo4 makes limited and nonspecific contacts with the replicating base pair, thus relaxing base selection. Dpo4 is also captured in the crystal translocating two template bases to the active site at once, suggesting a possible mechanism for bypassing thymine dimers.
About this Structure
1N48 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
Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypass replication., Ling H, Boudsocq F, Woodgate R, Yang W, Cell. 2001 Oct 5;107(1):91-102. PMID:11595188
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