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1mwj
From Proteopedia
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==Crystal Structure of a MUG-DNA pseudo substrate complex== | ==Crystal Structure of a MUG-DNA pseudo substrate complex== | ||
| - | <StructureSection load='1mwj' size='340' side='right' caption='[[1mwj]], [[Resolution|resolution]] 2.85Å' scene=''> | + | <StructureSection load='1mwj' size='340' side='right'caption='[[1mwj]], [[Resolution|resolution]] 2.85Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1mwj]] is a 2 chain structure with sequence from [ | + | <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> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85Å</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=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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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mw/1mwj_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mw/1mwj_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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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| - | 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:10581234<ref>PMID:10581234</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
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| - | ==See Also== | ||
| - | *[[DNA glycosylase|DNA glycosylase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Barrett | + | [[Category: Large Structures]] |
| - | [[Category: Brown | + | [[Category: Barrett TE]] |
| - | [[Category: Jiricny | + | [[Category: Brown T]] |
| - | [[Category: Pearl | + | [[Category: Jiricny J]] |
| - | [[Category: Savva | + | [[Category: Pearl LH]] |
| - | [[Category: Scharer | + | [[Category: Savva R]] |
| - | [[Category: Verdine | + | [[Category: Scharer O]] |
| - | + | [[Category: Verdine GL]] | |
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Current revision
Crystal Structure of a MUG-DNA pseudo substrate complex
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Categories: Escherichia coli | Large Structures | Barrett TE | Brown T | Jiricny J | Pearl LH | Savva R | Scharer O | Verdine GL

