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| <StructureSection load='4aia' size='340' side='right'caption='[[4aia]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='4aia' size='340' side='right'caption='[[4aia]], [[Resolution|resolution]] 1.80Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4aia]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AIA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AIA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4aia]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AIA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AIA FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><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></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jg6|2jg6]], [[4ai4|4ai4]], [[4ai5|4ai5]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr> |
- | <tr id='activity'><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 id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4aia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aia OCA], [https://pdbe.org/4aia PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aia RCSB], [https://www.ebi.ac.uk/pdbsum/4aia PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aia ProSAT]</span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4aia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aia OCA], [http://pdbe.org/4aia PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4aia RCSB], [http://www.ebi.ac.uk/pdbsum/4aia PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4aia ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| ==See Also== | | ==See Also== |
- | *[[DNA glycosylase|DNA glycosylase]] | + | *[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: DNA-3-methyladenine glycosylase I]] | + | [[Category: Large Structures]] |
- | [[Category: Naismith, J H]] | + | [[Category: Staphylococcus aureus]] |
- | [[Category: Yan, X]] | + | [[Category: Naismith JH]] |
- | [[Category: 3-methyladenine recognition]] | + | [[Category: Yan X]] |
- | [[Category: Dna repair]]
| + | |
- | [[Category: Hydrolase]]
| + | |
| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhu X, Yan X, Carter LG, Liu H, Graham S, Coote PJ, Naismith J. A model for 3-methyladenine recognition by 3-methyladenine DNA glycosylase I (TAG) from Staphylococcus aureus. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jun 1;68(Pt 6):610-5. Epub, 2012 May 22. PMID:22684054 doi:10.1107/S1744309112016363
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