1SL1
Binary 5' complex of T7 DNA polymerase with a DNA primer/template containing a cis-syn thymine dimer on the template
Summary for 1SL1
Entry DOI | 10.2210/pdb1sl1/pdb |
Related | 1SKR 1SKS 1SKW 1SL0 1SL2 1T7P |
Descriptor | 5'-D(*CP*GP*AP*AP*AP*AP*CP*GP*AP*CP*GP*GP*CP*CP*AP*GP*TP*GP*CP*CP*TP*(2DA))-3', 5'-D(*CP*CP*C*(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 Keywords | dna polymerase, fidelity, lesion bypass, thymine dimer, open, close, transferase-electron transport-dna complex, transferase/electron transport/dna |
Biological source | Enterobacteria phage T7 More |
Total number of polymer chains | 4 |
Total formula weight | 105462.94 |
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 citation | Li, 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: 15235589DOI: 10.1038/nsmb792 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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