1mwi: Difference between revisions
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New page: left|200px<br /><applet load="1mwi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mwi, resolution 2.35Å" /> '''Crystal structure of... |
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== | ==Crystal structure of a MUG-DNA product complex== | ||
G:U mismatches resulting from deamination of cytosine are the most common | <StructureSection load='1mwi' size='340' side='right'caption='[[1mwi]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35Å</td></tr> | |||
<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> | |||
<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> | |||
</table> | |||
== 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/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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1mwi" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Barlow | [[Category: Barlow T]] | ||
[[Category: Barrett | [[Category: Barrett TE]] | ||
[[Category: Brown | [[Category: Brown T]] | ||
[[Category: Jiricny | [[Category: Jiricny J]] | ||
[[Category: Panayotou | [[Category: Panayotou G]] | ||
[[Category: Pearl | [[Category: Pearl LH]] | ||
[[Category: Savva | [[Category: Savva R]] | ||
Latest revision as of 13:07, 1 July 2026
Crystal structure of a MUG-DNA product complex
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