The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites
| Autor: | John A. Tainer, Eric de La Fortelle, Solange Moréra, Michael A. Gorman, Paul S. Freemont, Clifford D. Mol, Ian D. Hickson, Dominic G. Rothwell |
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| Rok vydání: | 1997 |
| Předmět: |
Models
Molecular DNA Repair Protein Conformation Recombinant Fusion Proteins Carbon-Oxygen Lyases Molecular Sequence Data Crystallography X-Ray General Biochemistry Genetics and Molecular Biology AP endonuclease Endonuclease Bacterial Proteins DNA-(Apurinic or Apyrimidinic Site) Lyase Escherichia coli Animals Deoxyribonuclease I Humans AP site Amino Acid Sequence Binding site Molecular Biology Exonuclease III Binding Sites Sequence Homology Amino Acid General Immunology and Microbiology biology General Neuroscience Nuclear Proteins DNA Base excision repair Endonucleases DNA-(apurinic or apyrimidinic site) lyase Exodeoxyribonucleases Biochemistry biology.protein Cattle Oxidation-Reduction Sequence Alignment Research Article Protein Binding |
| Zdroj: | The EMBO Journal. 16:6548-6558 |
| ISSN: | 1460-2075 |
| DOI: | 10.1093/emboj/16.21.6548 |
| Popis: | The structure of the major human apurinic/ apyrimidinic endonuclease (HAP1) has been solved at 2.2 A resolution. The enzyme consists of two symmetrically related domains of similar topology and has significant structural similarity to both bovine DNase I and its Escherichia coli homologue exonuclease III (EXOIII). A structural comparison of these enzymes reveals three loop regions specific to HAP1 and EXOIII. These loop regions apparently act in DNA abasic site (AP) recognition and cleavage since DNase I, which lacks these loops, correspondingly lacks AP site specificity. The HAP1 structure furthermore suggests a mechanism for AP site binding which involves the recognition of the deoxyribose moiety in an extrahelical conformation, rather than a 'flipped-out' base opposite the AP site. |
| Databáze: | OpenAIRE |
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