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1mwi

From Proteopedia

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[[Image:1mwi.gif|left|200px]]<br /><applet load="1mwi" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mwi, resolution 2.35&Aring;" />
 
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'''Crystal structure of a MUG-DNA product complex'''<br />
 
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==Overview==
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==Crystal structure of a MUG-DNA product complex==
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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.
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<StructureSection load='1mwi' size='340' side='right'caption='[[1mwi]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<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>
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1MWI is a [http://en.wikipedia.org/wiki/Single_protein 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].
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</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>
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<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>
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==Reference==
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<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>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9489705 9489705]
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mw/1mwi_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1mwi ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Barlow, T.]]
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[[Category: Barlow T]]
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[[Category: Barrett, T E.]]
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[[Category: Barrett TE]]
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[[Category: Brown, T.]]
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[[Category: Brown T]]
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[[Category: Jiricny, J.]]
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[[Category: Jiricny J]]
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[[Category: Panayotou, G.]]
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[[Category: Panayotou G]]
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[[Category: Pearl, L H.]]
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[[Category: Pearl LH]]
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[[Category: Savva, R.]]
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[[Category: Savva R]]
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[[Category: abasic site]]
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[[Category: dna-glycosylase]]
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[[Category: nucleotide flipping]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:59:43 2008''
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Current revision

Crystal structure of a MUG-DNA product complex

PDB ID 1mwi

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