1ewn: Difference between revisions

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[[Image:1ewn.gif|left|200px]]


{{Structure
==CRYSTAL STRUCTURE OF THE HUMAN AAG DNA REPAIR GLYCOSYLASE COMPLEXED WITH 1,N6-ETHENOADENINE-DNA==
|PDB= 1ewn |SIZE=350|CAPTION= <scene name='initialview01'>1ewn</scene>, resolution 2.1&Aring;
<StructureSection load='1ewn' size='340' side='right'caption='[[1ewn]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene>
<table><tr><td colspan='2'>[[1ewn]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EWN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EWN FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/DNA-3-methyladenine_glycosylase_II DNA-3-methyladenine glycosylase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.21 3.2.2.21]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDA:3-[2-DEOXY-RIBOFURANOSYL]-3H-1,3,4,5A,8-PENTAAZA-AS-INDACENE-5-MONOPHOSPHATE'>EDA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=1ewn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ewn OCA], [https://pdbe.org/1ewn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ewn RCSB], [https://www.ebi.ac.uk/pdbsum/1ewn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ewn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/3MG_HUMAN 3MG_HUMAN] Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.
== 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/ew/1ewn_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/main_output.php?pdb_ID=1ewn ConSurf].
<div style="clear:both"></div>


'''CRYSTAL STRUCTURE OF THE HUMAN AAG DNA REPAIR GLYCOSYLASE COMPLEXED WITH 1,N6-ETHENOADENINE-DNA'''
==See Also==
 
*[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The human 3-methyladenine DNA glycosylase [alkyladenine DNA glycosylase (AAG)] catalyzes the first step of base excision repair by cleaving damaged bases from DNA. Unlike other DNA glycosylases that are specific for a particular type of damaged base, AAG excises a chemically diverse selection of substrate bases damaged by alkylation or deamination. The 2.1-A crystal structure of AAG complexed to DNA containing 1,N(6)-ethenoadenine suggests how modified bases can be distinguished from normal DNA bases in the enzyme active site. Mutational analyses of residues contacting the alkylated base in the crystal structures suggest that the shape of the damaged base, its hydrogen-bonding characteristics, and its aromaticity all contribute to the selective recognition of damage by AAG.
 
==Disease==
Known disease associated with this structure: Opitz G syndrome, type I OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300552 300552]]
 
==About this Structure==
1EWN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EWN OCA].
 
==Reference==
Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG., Lau AY, Wyatt MD, Glassner BJ, Samson LD, Ellenberger T, Proc Natl Acad Sci U S A. 2000 Dec 5;97(25):13573-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11106395 11106395]
[[Category: DNA-3-methyladenine glycosylase II]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Ellenberger, T.]]
[[Category: Ellenberger T]]
[[Category: Glassner, B J.]]
[[Category: Glassner BJ]]
[[Category: Lau, A Y.]]
[[Category: Lau AY]]
[[Category: Samson, L D.]]
[[Category: Samson LD]]
[[Category: Wyatt, M D.]]
[[Category: Wyatt MD]]
[[Category: NA]]
[[Category: 3-methyladenine dna glycosylase]]
[[Category: aag]]
[[Category: anpg]]
[[Category: dna repair]]
[[Category: glycosylase]]
[[Category: mpg]]
 
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Retrieved from "https://proteopedia.org/1ewn"