4ai4: Difference between revisions
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< | ==crystal structure of E38Q mutant of 3-methyladenine DNA glycosylase I from Staphylococcus aureus== | ||
<StructureSection load='4ai4' size='340' side='right'caption='[[4ai4]], [[Resolution|resolution]] 1.73Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ai4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_MSSA476 Staphylococcus aureus subsp. aureus MSSA476]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AI4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AI4 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.73Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ai4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ai4 OCA], [https://pdbe.org/4ai4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ai4 RCSB], [https://www.ebi.ac.uk/pdbsum/4ai4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ai4 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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 A 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. | |||
A model for 3-methyladenine recognition by 3-methyladenine DNA glycosylase I (TAG) from Staphylococcus aureus.,Zhu X, Yan X, Carter LG, Liu H, Graham S, Coote PJ, Naismith J Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jun 1;68(Pt 6):610-5. Epub, 2012 May 22. PMID:22684054<ref>PMID:22684054</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4ai4" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]] | ||
[[Category: | == References == | ||
[[Category: Staphylococcus aureus subsp. aureus | <references/> | ||
[[Category: Naismith | __TOC__ | ||
[[Category: Zhu | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Staphylococcus aureus subsp. aureus MSSA476]] | |||
[[Category: Naismith JH]] | |||
[[Category: Zhu X]] | |||
Latest revision as of 11:27, 20 December 2023
crystal structure of E38Q mutant of 3-methyladenine DNA glycosylase I from Staphylococcus aureus
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