4AI4
crystal structure of E38Q mutant of 3-methyladenine DNA glycosylase I from Staphylococcus aureus
Summary for 4AI4
| Entry DOI | 10.2210/pdb4ai4/pdb |
| Related | 2JG6 4AI5 |
| Descriptor | DNA-3-METHYLADENINE GLYCOSYLASE I, ZINC ION, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | hydrolase, dna repair |
| Biological source | STAPHYLOCOCCUS AUREUS SUBSP. AUREUS MSSA476 |
| Total number of polymer chains | 1 |
| Total formula weight | 21830.03 |
| Authors | Zhu, X.,Naismith, J.H. (deposition date: 2012-02-08, release date: 2012-02-15, Last modification date: 2023-12-20) |
| Primary citation | Zhu, X.,Yan, X.,Carter, L.G.,Liu, H.,Graham, S.,Coote, P.J.,Naismith, J. A Model for 3-Methyladenine Recognition by 3-Methyladenine DNA Glycosylase I (Tag) from Staphylococcus Aureus. Acta Crystallogr.,Sect.F, 68:610-, 2012 Cited by PubMed Abstract: The removal of chemically damaged DNA bases such as 3-methyladenine (3-MeA) is an essential process in all living organisms and is catalyzed by the enzyme 3-MeA DNA glycosylase I. A key question is how the enzyme selectively recognizes the alkylated 3-MeA over the much more abundant adenine. The crystal structures of native and Y16F-mutant 3-MeA DNA glycosylase I from Staphylococcus aureus in complex with 3-MeA are reported to 1.8 and 2.2 Å resolution, respectively. Isothermal titration calorimetry shows that protonation of 3-MeA decreases its binding affinity, confirming previous fluorescence studies that show that charge-charge recognition is not critical for the selection of 3-MeA over adenine. It is hypothesized that the hydrogen-bonding pattern of Glu38 and Tyr16 of 3-MeA DNA glycosylase I with a particular tautomer unique to 3-MeA contributes to recognition and selection. PubMed: 22684054DOI: 10.1107/S1744309112016363 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.73 Å) |
Structure validation
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