Structural characterization of human 8-oxoguanine DNA glycosylase variants bearing active site mutations
Open accessAbstract
The human 8-oxoguanine DNA glycosylase (hOGG1) protein is responsible for initiating base excision DNA repair of the endogenous mutagen 8-oxoguanine. Like nearly all DNA glycosylases, hOGG1 extrudes its substrate from the DNA helix and inserts it into an extrahelical enzyme active site pocket lined with residues that participate in lesion recognition and catalysis. Structural analysis has been performed on mutant versions of hOGG1 having changes in catalytic residues but not on variants having altered 7,8-dihydro-8-oxoguanine (oxoG) contact residues. Here we report high resolution structural analysis of such recognition variants. We found that Ala substitution at residues that contact the phosphate 5' to the lesion (H270A mutation) and its Watson-Crick face (Q315A mutation) simply removed key functionality from the contact interface but otherwise had no effect on structure. Ala substitution at the only residue making an oxoG-specific contact (G42A mutation) introduced torsional stress into the DNA contact surface of hOGG1, but this was overcome by local interactions within the folded protein, indicating that this oxoG recognition motif is "hardwired." Introduction of a side chain intended to sterically obstruct the active site pocket (Q315F mutation) led to two different structures, one of which (Q315F(*149)) has the oxoG lesion in an exosite flanking the active site and the other of which (Q315F(*292)) has the oxoG inserted nearly completely into the lesion recognition pocket. The latter structure offers a view of the latest stage in the base extrusion pathway yet observed, and its lack of catalytic activity demonstrates that the transition state for displacement of the lesion base is geometrically demanding.
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Structures of DNA in complex with OGG1 exist in a catalytically active form for 8oxoG that is adjacent to guanine only in the 5'-position in -AGGT- sequences.
“In fact, the structures of DNA in complex with N-glycosylase/DNA lyase (OGG1), which is a base-excision repair enzyme for 8oxoG, exist in a catalytically active form for 8oxoG that is adjacent to guanine only in the 5’-position in -AGGT- sequences (S12 Fig) [40,48–51].”
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Thermodynamic analysis of fast stages of specific lesion recognition by DNA repair enzymes
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Singlet oxygen-induced covalent trapping of G4-binding peptides onto their cognate target G4
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REPAIR AND EFFECTS OF THE 8-OXOG LESION IN DNA
Covino, J. (2007) · The Mathematics Enthusiast
- Authors
- Radom, C. T., Banerjee, A., & Verdine, G. L.
- Affiliations
- Harvard University (US)
- Corresponding author
- Verdine, Gregory L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2007-03
- Volume
- 282
- Issue
- 12
- Pages
- 9182-9194
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2103089225
- Cited by
- 75
- References
- 43
- Citations by year
- 2026: 5 · 2025: 1 · 2024: 4 · 2023: 1 · 2022: 3 · 2021: 1 · 2020: 6 · 2019: 4 · 2018: 2 · 2017: 6 · 2016: 2 · 2015: 2 · 2014: 6 · 2013: 4 · 2012: 6
- FWCI
- 2.17
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Energy (31-109-ENG-38, DEAC-02-98CH10886, -AC02-98 CH 10886, DE-AC02-)
- National Institutes of Health (DE-AC02-98CH10886, W-31-109-ENG-38)
- Office of Science (DE-AC-02-98CH10886, DE-AC02, 31-109-ENG-38)
- National Cancer Institute (CA 100742, R01CA100742)
- Basic Energy Sciences (DE-AC02, DEAC0298CH10886, AC02-98CH10886)
- Biological and Environmental Research (W-31-109-ENG, DE-AC02-98CH10886, W-31-109-ENG-38)
- Argonne National Laboratory (DE-AC02)
- Brookhaven National Laboratory (AC-02-98CH10886, DE-AC02- 98CH10886)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Keywords
- OGG1, DNA base excision repair, 8-oxoguanine, lesion recognition, active site pocket, catalytic residues, torsional stress, exosite
- MeSH terms
- Alanine, Binding Sites, Catalysis, Cloning, Molecular, Cross-Linking Reagents, Humans, Models, Chemical, Models, Molecular, Molecular Conformation, Mutation, Protein Conformation, Protein Structure, Tertiary, Crystallography, X-Ray, Amino Acid Motifs, DNA Glycosylases
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