3LQC
X-ray crystal structure of oxidized XRCC1 bound to DNA pol beta Palm thumb domain
Summary for 3LQC
| Entry DOI | 10.2210/pdb3lqc/pdb |
| Related | 3K75 3K77 |
| Descriptor | DNA repair protein XRCC1, DNA polymerase beta, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | allosteric disulfide, scaffolding protein, dna repair, dna damage, nucleus, phosphoprotein, polymorphism, dna replication, dna synthesis, dna-binding, dna-directed dna polymerase, lyase, magnesium, metal-binding, nucleotidyltransferase, sodium, transferase, dna-binding protein, dna binding protein |
| Biological source | Homo sapiens (human) More |
| Cellular location | Nucleus: P18887 P06766 |
| Total number of polymer chains | 2 |
| Total formula weight | 44667.04 |
| Authors | Cuneo, M.J.,Krahn, J.M.,London, R.E. (deposition date: 2010-02-09, release date: 2010-04-28, Last modification date: 2023-09-06) |
| Primary citation | Cuneo, M.J.,London, R.E. Oxidation state of the XRCC1 N-terminal domain regulates DNA polymerase beta binding affinity. Proc.Natl.Acad.Sci.USA, 107:6805-6810, 2010 Cited by PubMed Abstract: Formation of a complex between the XRCC1 N-terminal domain (NTD) and DNA polymerase beta (Pol beta) is central to base excision repair of damaged DNA. Two crystal forms of XRCC1-NTD complexed with Pol beta have been solved, revealing that the XRCC1-NTD is able to adopt a redox-dependent alternate fold, characterized by a disulfide bond, and substantial variations of secondary structure, folding topology, and electrostatic surface. Although most of these structural changes occur distal to the interface, the oxidized XRCC1-NTD forms additional interactions with Pol beta, enhancing affinity by an order of magnitude. Transient disulfide bond formation is increasingly recognized as an important molecular regulatory mechanism. The results presented here suggest a paradigm in DNA repair in which the redox state of a scaffolding protein plays an active role in organizing the repair complex. PubMed: 20351257DOI: 10.1073/pnas.0914077107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.349 Å) |
Structure validation
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