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1mwj

From Proteopedia

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[[Image:1mwj.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of a MUG-DNA pseudo substrate complex==
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|PDB= 1mwj |SIZE=350|CAPTION= <scene name='initialview01'>1mwj</scene>, resolution 2.85&Aring;
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<StructureSection load='1mwj' size='340' side='right'caption='[[1mwj]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <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>, <scene name='pdbligand=DU:2&#39;-DEOXYURIDINE-5&#39;-MONOPHOSPHATE'>DU</scene>
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<table><tr><td colspan='2'>[[1mwj]] 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=1MWJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MWJ FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.85&#8491;</td></tr>
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|GENE= MUG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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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=1mwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwj OCA], [https://pdbe.org/1mwj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mwj RCSB], [https://www.ebi.ac.uk/pdbsum/1mwj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mwj ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1mug|1MUG]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwj OCA], [http://www.ebi.ac.uk/pdbsum/1mwj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mwj RCSB]</span>
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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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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''Crystal Structure of a MUG-DNA pseudo substrate complex'''
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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/1mwj_consurf.spt"</scriptWhenChecked>
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==Overview==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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The bacterial mismatch-specific uracil-DNA glycosylase (MUG) and eukaryotic thymine-DNA glycosylase (TDG) enzymes form a homologous family of DNA glycosylases that initiate base-excision repair of G:U/T mismatches. Despite low sequence homology, the MUG/TDG enzymes are structurally related to the uracil-DNA glycosylase enzymes, but have a very different mechanism for substrate recognition. We have now determined the crystal structure of the Escherichia coli MUG enzyme complexed with an oligonucleotide containing a non-hydrolysable deoxyuridine analogue mismatched with guanine, providing the first structure of an intact substrate-nucleotide productively bound to a hydrolytic DNA glycosylase. The structure of this complex explains the preference for G:U over G:T mispairs, and reveals an essentially non-specific pyrimidine-binding pocket that allows MUG/TDG enzymes to excise the alkylated base, 3, N(4)-ethenocytosine. Together with structures for the free enzyme and for an abasic-DNA product complex, the MUG-substrate analogue complex reveals the conformational changes accompanying the catalytic cycle of substrate binding, base excision and product release.
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==About this Structure==
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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=1mwj ConSurf].
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1MWJ 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=1MWJ OCA].
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<div style="clear:both"></div>
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== References ==
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==Reference==
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<references/>
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Crystal structure of a thwarted mismatch glycosylase DNA repair complex., Barrett TE, Scharer OD, Savva R, Brown T, Jiricny J, Verdine GL, Pearl LH, EMBO J. 1999 Dec 1;18(23):6599-609. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10581234 10581234]
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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: 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: 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: Scharer, O.]]
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[[Category: Scharer O]]
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[[Category: Verdine, G L.]]
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[[Category: Verdine GL]]
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[[Category: non-hydrolysable dna-complex]]
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[[Category: rossmann fold]]
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[[Category: uracil recognition.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:22:06 2008''
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Current revision

Crystal Structure of a MUG-DNA pseudo substrate complex

PDB ID 1mwj

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