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1lmz
From Proteopedia
(Difference between revisions)
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| - | [[ | + | ==Solution Structure of 3-Methyladenine DNA Glycosylase I (TAG)== |
| + | <StructureSection load='1lmz' size='340' side='right' caption='[[1lmz]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1lmz]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LMZ FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TAG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=37762 Escherichia coli B])</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=1lmz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lmz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1lmz RCSB], [http://www.ebi.ac.uk/pdbsum/1lmz PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <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> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | ||
| - | + | ||
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| - | + | ||
==See Also== | ==See Also== | ||
| - | *[[DNA | + | *[[DNA glycosylase|DNA glycosylase]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: DNA-3-methyladenine glycosylase I]] | [[Category: DNA-3-methyladenine glycosylase I]] | ||
[[Category: Escherichia coli b]] | [[Category: Escherichia coli b]] | ||
Revision as of 08:37, 3 October 2014
Solution Structure of 3-Methyladenine DNA Glycosylase I (TAG)
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