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


{{Structure
==G:T/U MISMATCH-SPECIFIC DNA GLYCOSYLASE FROM E.COLI==
|PDB= 1mug |SIZE=350|CAPTION= <scene name='initialview01'>1mug</scene>, resolution 1.80&Aring;
<StructureSection load='1mug' size='340' side='right'caption='[[1mug]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
<table><tr><td colspan='2'>[[1mug]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MUG FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mug OCA], [https://pdbe.org/1mug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mug RCSB], [https://www.ebi.ac.uk/pdbsum/1mug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mug ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mug OCA], [http://www.ebi.ac.uk/pdbsum/1mug PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mug RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/MUG_ECOLI MUG_ECOLI] Excises ethenocytosine and uracil, which can arise by alkylation or deamination of cytosine, respectively, from the corresponding mispairs with guanine in ds-DNA. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine functions in substrate recognition. Required for DNA damage lesion repair in stationary-phase cells.<ref>PMID:8878487</ref> <ref>PMID:12668677</ref>
== 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/mu/1mug_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=1mug ConSurf].
<div style="clear:both"></div>


'''G:T/U MISMATCH-SPECIFIC DNA GLYCOSYLASE FROM E.COLI'''
==See Also==
 
*[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]]
 
== References ==
==Overview==
<references/>
G:U mismatches resulting from deamination of cytosine are the most common promutagenic lesions occurring in DNA. Uracil is removed in a base-excision repair pathway by uracil DNA-glycosylase (UDG), which excises uracil from both single- and double-stranded DNA. Recently, a biochemically distinct family of DNA repair enzymes has been identified, which excises both uracil and thymine, but only from mispairs with guanine. Crystal structures of the mismatch-specific uracil DNA-glycosylase (MUG) from E. coli, and of a DNA complex, reveal a remarkable structural and functional homology to UDGs despite low sequence identity. Details of the MUG structure explain its thymine DNA-glycosylase activity and the specificity for G:U/T mispairs, which derives from direct recognition of guanine on the complementary strand.
__TOC__
 
</StructureSection>
==About this Structure==
1MUG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MUG OCA].
 
==Reference==
Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions., Barrett TE, Savva R, Panayotou G, Barlow T, Brown T, Jiricny J, Pearl LH, Cell. 1998 Jan 9;92(1):117-29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9489705 9489705]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Barlow, T.]]
[[Category: Barlow T]]
[[Category: Barrett, T E.]]
[[Category: Barrett TE]]
[[Category: Brown, T.]]
[[Category: Brown T]]
[[Category: Jiricny, J.]]
[[Category: Jiricny J]]
[[Category: Panayotou, G.]]
[[Category: Panayotou G]]
[[Category: Pearl, L H.]]
[[Category: Pearl LH]]
[[Category: Savva, R.]]
[[Category: Savva R]]
[[Category: dna-glycosylase]]
 
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