Show simple item record

Files in this item

Thumbnail

Item metadata

dc.contributor.authorZhu, Xiaofeng
dc.contributor.authorYan, Xuan
dc.contributor.authorCarter, Lester G.
dc.contributor.authorLiu, Huanting
dc.contributor.authorGraham, Shirley
dc.contributor.authorCoote, Peter J.
dc.contributor.authorNaismith, James
dc.date.accessioned2012-12-14T16:01:02Z
dc.date.available2012-12-14T16:01:02Z
dc.date.issued2012-06
dc.identifier.citationZhu , 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/S1744309112016363en
dc.identifier.issn1744-3091
dc.identifier.otherPURE: 28219867
dc.identifier.otherPURE UUID: d6c9d916-b470-4de9-9319-d8da48d7729a
dc.identifier.otherWOS: 000305073600001
dc.identifier.otherScopus: 84862214827
dc.identifier.otherORCID: /0000-0001-5190-805X/work/40963217
dc.identifier.urihttps://hdl.handle.net/10023/3302
dc.description.abstractThe 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.extent6
dc.language.isoeng
dc.relation.ispartofActa Crystallographica. Section F, Structural biology and crystallization communicationsen
dc.rightsCopyright © International Union of Crystallography.en
dc.subject3-methyladenine DNA glycosylase Ien
dc.subjectFluorescence measurementsen
dc.subjectITCen
dc.subjectDNA repairen
dc.subjectRecognitionen
dc.subjectQD Chemistryen
dc.subject.lccQDen
dc.titleA model for 3-methyladenine recognition by 3-methyladenine DNA glycosylase I (TAG) from Staphylococcus aureusen
dc.typeJournal articleen
dc.contributor.sponsorBBSRCen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.contributor.institutionUniversity of St Andrews. EaSTCHEMen
dc.identifier.doihttps://doi.org/10.1107/S1744309112016363
dc.description.statusPeer revieweden
dc.identifier.grantnumberBBS/B/14426en


This item appears in the following Collection(s)

Show simple item record