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


{{Structure
==Crystal structure of a MUG-DNA product complex==
|PDB= 1mwi |SIZE=350|CAPTION= <scene name='initialview01'>1mwi</scene>, resolution 2.35&Aring;
<StructureSection load='1mwi' size='340' side='right'caption='[[1mwi]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=AAB:2-DEOXY-5-PHOSPHORIBOSE+GROUP'>AAB</scene>, <scene name='pdbligand=DA:2&#39;-DEOXYADENOSINE-5&#39;-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2&#39;-DEOXYGUANOSINE-5&#39;-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>
<table><tr><td colspan='2'>[[1mwi]] is a 2 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=1MWI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MWI 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]] 2.35&#8491;</td></tr>
|GENE= MUG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AAB:2-DEOXY-RIBOFURANOSE-5-MONOPHOSPHATE'>AAB</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=1mwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwi OCA], [https://pdbe.org/1mwi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mwi RCSB], [https://www.ebi.ac.uk/pdbsum/1mwi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mwi ProSAT]</span></td></tr>
|RELATEDENTRY=[[1mug|1MUG]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwi OCA], [http://www.ebi.ac.uk/pdbsum/1mwi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mwi 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 ==
'''Crystal structure of a MUG-DNA product complex'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mw/1mwi_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1mwi ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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.


==About this Structure==
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:9489705<ref>PMID:9489705</ref>
1MWI 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=1MWI OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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]
</div>
<div class="pdbe-citations 1mwi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[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: abasic site]]
[[Category: dna-glycosylase]]
[[Category: nucleotide flipping]]
 
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Retrieved from "https://proteopedia.org/1mwi"