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]] | ||
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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. | ||
- | + | ==See Also== | |
- | + | *[[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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