1lmz
From Proteopedia
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==Solution Structure of 3-Methyladenine DNA Glycosylase I (TAG)== | ==Solution Structure of 3-Methyladenine DNA Glycosylase I (TAG)== | ||
| - | <StructureSection load='1lmz' size='340' side='right' caption='[[1lmz | + | <StructureSection load='1lmz' size='340' side='right'caption='[[1lmz]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1lmz]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1lmz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_B Escherichia coli B]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LMZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LMZ FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1lmz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lmz OCA], [https://pdbe.org/1lmz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lmz RCSB], [https://www.ebi.ac.uk/pdbsum/1lmz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lmz ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/3MG1_ECOLI 3MG1_ECOLI] Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine from the damaged DNA polymer formed by alkylation lesions. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lm/1lmz_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lm/1lmz_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lmz ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lmz ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The Escherichia coli enzyme 3-methyladenine DNA glycosylase I (TAG) hydrolyzes the glycosidic bond of 3-methyladenine (3-MeA) in DNA and is found in many bacteria and some higher eukaryotes. TAG shows little primary sequence identity with members of the well-known helix-hairpin-helix (HhH) superfamily of DNA repair glycosylases, which consists of AlkA, EndoIII, MutY and hOGG1. Unexpectedly, the three-dimensional solution structure reported here reveals TAG as member of this superfamily. The restricted specificity of TAG for 3-MeA bases probably arises from its unique aromatic rich 3-MeA binding pocket and the absence of a catalytic aspartate that is present in all other HhH family members. | ||
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| - | 3-Methyladenine DNA glycosylase I is an unexpected helix-hairpin-helix superfamily member.,Drohat AC, Kwon K, Krosky DJ, Stivers JT Nat Struct Biol. 2002 Sep;9(9):659-64. PMID:12161745<ref>PMID:12161745</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1lmz" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[DNA glycosylase|DNA glycosylase]] | + | *[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]] |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli B]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Drohat AC]] |
| - | [[Category: | + | [[Category: Krosky DJ]] |
| - | [[Category: | + | [[Category: Kwon K]] |
| - | [[Category: | + | [[Category: Stivers JT]] |
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Current revision
Solution Structure of 3-Methyladenine DNA Glycosylase I (TAG)
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