View source for 6tc9


==Crystal structure of MutM from Neisseria meningitidis==
<StructureSection load='6tc9' size='340' side='right'caption='[[6tc9]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6tc9]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_alpha522 Neisseria meningitidis alpha522] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TC9 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]] 2.175&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3DR:1,2-DIDEOXYRIBOFURANOSE-5-PHOSPHATE'>3DR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6tc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tc9 OCA], [https://pdbe.org/6tc9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tc9 RCSB], [https://www.ebi.ac.uk/pdbsum/6tc9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tc9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/I4E596_NEIME I4E596_NEIME] Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.[HAMAP-Rule:MF_00103]
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== Publication Abstract from PubMed ==
Bacterial MutM is a DNA repair glycosylase removing DNA damage generated from oxidative stress and, therefore, preventing mutations and genomic instability. MutM belongs to the Fpg/Nei family of prokaryotic enzymes sharing structural and functional similarities with their eukaryotic counterparts, for example, NEIL1-NEIL3. Here, we present two crystal structures of MutM from pathogenic Neisseria meningitidis: a MutM holoenzyme and MutM bound to DNA. The free enzyme exists in an open conformation, while upon binding to DNA, both the enzyme and DNA undergo substantial structural changes and domain rearrangement. Our data show that not only NEI glycosylases but also the MutMs undergo dramatic conformational changes. Moreover, crystallographic data support the previously published observations that MutM enzymes are rather flexible and dynamic molecules.

Conformational changes of DNA repair glycosylase MutM triggered by DNA binding.,Landova B, Silhan J FEBS Lett. 2020 Jun 29. doi: 10.1002/1873-3468.13876. PMID:32598485<ref>PMID:32598485</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6tc9" style="background-color:#fffaf0;"></div>

==See Also==
*[[DNA glycosylase 3D structures|DNA glycosylase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Neisseria meningitidis alpha522]]
[[Category: Synthetic construct]]
[[Category: Boura E]]
[[Category: Landova B]]
[[Category: Silhan J]]