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1SKW

Binary 3' complex of T7 DNA polymerase with a DNA primer/template containing a disordered cis-syn thymine dimer on the template

Summary for 1SKW
Entry DOI10.2210/pdb1skw/pdb
Related1SKR 1SKS 1SL0 1SL1 1SL2 1T7P
Descriptor5'-D(*CP*GP*AP*AP*AP*AP*CP*GP*AP*C*GP*GP*CP*CP*AP*GP*TP*GP*CP*CP*(2DT))-3', 5'-D(*CP*CP*CP*(TTD)P*AP*GP*GP*CP*AP*CP*TP*GP*GP*CP*CP*GP*TP*CP*GP*TP*TP*TP*TP*CP*G)-3', DNA polymerase, ... (6 entities in total)
Functional Keywordsdna polymerase, fidelity, lesion bypass, thymine dimer, open, close, transferase-electron transport-dna complex, transferase/electron transport/dna
Biological sourceEnterobacteria phage T7
More
Total number of polymer chains4
Total formula weight105149.74
Authors
Li, Y.,Dutta, S.,Doublie, S.,Bdour, H.M.,Taylor, J.S.,Ellenberger, T. (deposition date: 2004-03-05, release date: 2004-07-06, Last modification date: 2024-02-14)
Primary citationLi, Y.,Dutta, S.,Doublie, S.,Bdour, H.M.,Taylor, J.S.,Ellenberger, T.
Nucleotide insertion opposite a cis-syn thymine dimer by a replicative DNA polymerase from bacteriophage T7.
Nat.Struct.Mol.Biol., 11:784-790, 2004
Cited by
PubMed Abstract: Ultraviolet-induced DNA damage poses a lethal block to replication. To understand the structural basis for this, we determined crystal structures of a replicative DNA polymerase from bacteriophage T7 in complex with nucleotide substrates and a DNA template containing a cis-syn cyclobutane pyrimidine dimer (CPD). When the 3' thymine is the templating base, the CPD is rotated out of the polymerase active site and the fingers subdomain adopts an open orientation. When the 5' thymine is the templating base, the CPD lies within the polymerase active site where it base-pairs with the incoming nucleotide and the 3' base of the primer, while the fingers are in a closed conformation. These structures reveal the basis for the strong block of DNA replication that is caused by this photolesion.
PubMed: 15235589
DOI: 10.1038/nsmb792
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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數據於2024-11-13公開中

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