6BTE
DNA Polymerase Beta I260Q Binary Complex
Summary for 6BTE
| Entry DOI | 10.2210/pdb6bte/pdb |
| Descriptor | DNA polymerase beta, DNA Template Strand, DNA Primer Strand, ... (8 entities in total) |
| Functional Keywords | lyase, dna complex, transferase, lyase-dna complex, lyase/dna |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 48042.08 |
| Authors | Eckenroth, B.E.,Doublie, S. (deposition date: 2017-12-06, release date: 2018-09-26, Last modification date: 2023-10-04) |
| Primary citation | Liptak, C.,Mahmoud, M.M.,Eckenroth, B.E.,Moreno, M.V.,East, K.,Alnajjar, K.S.,Huang, J.,Towle-Weicksel, J.B.,Doublie, S.,Loria, J.P.,Sweasy, J.B. I260Q DNA polymerase beta highlights precatalytic conformational rearrangements critical for fidelity. Nucleic Acids Res., 46:10740-10756, 2018 Cited by PubMed Abstract: DNA polymerase β (pol β) fills single nucleotide gaps in DNA during base excision repair and non-homologous end-joining. Pol β must select the correct nucleotide from among a pool of four nucleotides with similar structures and properties in order to maintain genomic stability during DNA repair. Here, we use a combination of X-ray crystallography, fluorescence resonance energy transfer and nuclear magnetic resonance to show that pol β's ability to access the appropriate conformations both before and upon binding to nucleotide substrates is integral to its fidelity. Importantly, we also demonstrate that the inability of the I260Q mutator variant of pol β to properly navigate this conformational landscape results in error-prone DNA synthesis. Our work reveals that precatalytic conformational rearrangements themselves are an important underlying mechanism of substrate selection by DNA pol β. PubMed: 30239932DOI: 10.1093/nar/gky825 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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