4ai5: Difference between revisions
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[[ | ==Crystal structure of Y16F of 3-methyladenine DNA glycosylase I (TAG) in complex with 3-methyladenine== | ||
<StructureSection load='4ai5' size='340' side='right' caption='[[4ai5]], [[Resolution|resolution]] 2.22Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ai5]] is a 5 chain structure with sequence from [http://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=4AI5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AI5 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADK:3-METHYL-3H-PURIN-6-YLAMINE'>ADK</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jg6|2jg6]], [[4ai4|4ai4]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-3-methyladenine_glycosylase_I DNA-3-methyladenine glycosylase I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.20 3.2.2.20] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ai5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ai5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ai5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ai5 PDBsum]</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> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: DNA-3-methyladenine glycosylase I]] | [[Category: DNA-3-methyladenine glycosylase I]] | ||
[[Category: Staphylococcus aureus subsp. aureus mssa476]] | [[Category: Staphylococcus aureus subsp. aureus mssa476]] | ||
