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1mwj

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Revision as of 15:02, 12 October 2017

Crystal Structure of a MUG-DNA pseudo substrate complex

Structural highlights

1mwj is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	1mug
Gene:	MUG ("Bacillus coli" Migula 1895)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gallinari P, Jiricny J. A new class of uracil-DNA glycosylases related to human thymine-DNA glycosylase. Nature. 1996 Oct 24;383(6602):735-8. PMID:8878487 doi:http://dx.doi.org/10.1038/383735a0
↑ O'Neill RJ, Vorob'eva OV, Shahbakhti H, Zmuda E, Bhagwat AS, Baldwin GS. Mismatch uracil glycosylase from Escherichia coli: a general mismatch or a specific DNA glycosylase? J Biol Chem. 2003 Jun 6;278(23):20526-32. Epub 2003 Mar 31. PMID:12668677 doi:http://dx.doi.org/10.1074/jbc.M210860200
↑ Barrett TE, Scharer OD, Savva R, Brown T, Jiricny J, Verdine GL, Pearl LH. Crystal structure of a thwarted mismatch glycosylase DNA repair complex. EMBO J. 1999 Dec 1;18(23):6599-609. PMID:10581234 doi:10.1093/emboj/18.23.6599

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1mwj"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of a MUG-DNA pseudo substrate complex==
 <StructureSection load='1mwj' size='340' side='right' caption='[[1mwj]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mug|1mug]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MUG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1mwj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mwj RCSB], [http://www.ebi.ac.uk/pdbsum/1mwj PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1mwj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mwj RCSB], [http://www.ebi.ac.uk/pdbsum/1mwj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mwj ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1mwj" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[DNA glycosylase|DNA glycosylase]]
 == References ==
 <references/>

1mwj

From Proteopedia

Revision as of 15:02, 12 October 2017

Crystal Structure of a MUG-DNA pseudo substrate complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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