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A model for 3-methyladenine recognition by 3-methyladenine DNA glycosylase I (TAG) from Staphylococcus aureus
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dc.contributor.author | Zhu, Xiaofeng | |
dc.contributor.author | Yan, Xuan | |
dc.contributor.author | Carter, Lester G. | |
dc.contributor.author | Liu, Huanting | |
dc.contributor.author | Graham, Shirley | |
dc.contributor.author | Coote, Peter J. | |
dc.contributor.author | Naismith, James | |
dc.date.accessioned | 2012-12-14T16:01:02Z | |
dc.date.available | 2012-12-14T16:01:02Z | |
dc.date.issued | 2012-06 | |
dc.identifier.citation | Zhu , X , Yan , X , Carter , L G , Liu , H , Graham , S , Coote , P J & Naismith , J 2012 , ' A model for 3-methyladenine recognition by 3-methyladenine DNA glycosylase I (TAG) from Staphylococcus aureus ' , Acta Crystallographica. Section F, Structural biology and crystallization communications , vol. 68 , pp. 610-615 . https://doi.org/10.1107/S1744309112016363 | en |
dc.identifier.issn | 1744-3091 | |
dc.identifier.other | PURE: 28219867 | |
dc.identifier.other | PURE UUID: d6c9d916-b470-4de9-9319-d8da48d7729a | |
dc.identifier.other | WOS: 000305073600001 | |
dc.identifier.other | Scopus: 84862214827 | |
dc.identifier.other | ORCID: /0000-0001-5190-805X/work/40963217 | |
dc.identifier.uri | https://hdl.handle.net/10023/3302 | |
dc.description.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 angstrom resolution, respectively. Isothermal titration calorimetry shows that protonation of 3-MeA decreases its binding affinity, confirming previous fluorescence studies that show that chargecharge 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. | |
dc.format.extent | 6 | |
dc.language.iso | eng | |
dc.relation.ispartof | Acta Crystallographica. Section F, Structural biology and crystallization communications | en |
dc.rights | Copyright © International Union of Crystallography. | en |
dc.subject | 3-methyladenine DNA glycosylase I | en |
dc.subject | Fluorescence measurements | en |
dc.subject | ITC | en |
dc.subject | DNA repair | en |
dc.subject | Recognition | en |
dc.subject | QD Chemistry | en |
dc.subject.lcc | QD | en |
dc.title | A model for 3-methyladenine recognition by 3-methyladenine DNA glycosylase I (TAG) from Staphylococcus aureus | en |
dc.type | Journal article | en |
dc.contributor.sponsor | BBSRC | en |
dc.description.version | Publisher PDF | en |
dc.contributor.institution | University of St Andrews. School of Biology | en |
dc.contributor.institution | University of St Andrews. Biomedical Sciences Research Complex | en |
dc.contributor.institution | University of St Andrews. School of Chemistry | en |
dc.contributor.institution | University of St Andrews. EaSTCHEM | en |
dc.identifier.doi | https://doi.org/10.1107/S1744309112016363 | |
dc.description.status | Peer reviewed | en |
dc.identifier.grantnumber | BBS/B/14426 | en |
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