5z41

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==Aquifex aeolicus MutL endonuclease domain with a single zinc ion.==
==Aquifex aeolicus MutL endonuclease domain with a single zinc ion.==
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<StructureSection load='5z41' size='340' side='right' caption='[[5z41]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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<StructureSection load='5z41' size='340' side='right'caption='[[5z41]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5z41]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z41 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z41 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5z41]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z41 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Z41 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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]] 1.7&#8491;</td></tr>
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<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=5z41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z41 OCA], [http://pdbe.org/5z41 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z41 RCSB], [http://www.ebi.ac.uk/pdbsum/5z41 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z41 ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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=5z41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z41 OCA], [https://pdbe.org/5z41 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5z41 RCSB], [https://www.ebi.ac.uk/pdbsum/5z41 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5z41 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MUTL_AQUAE MUTL_AQUAE]] This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a "molecular matchmaker", a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex (By similarity).
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[https://www.uniprot.org/uniprot/MUTL_AQUAE MUTL_AQUAE] This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a "molecular matchmaker", a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The DNA mismatch repair endonuclease MutL consists of N-terminal ATPase and C-terminal endonuclease domains. The endonuclease domain binds zinc ion, although the ion seems not to function as a catalytic metal ion. Here, we solved the crystal structures of the Aquifex aeolicus MutL (aqMutL) endonuclease domain complexed with a single and three zinc ions. Differences between the two structures show that binding of multiple zinc ions induces a closed-to-open conformational change at the catalytic site. It is also revealed that the three-zinc-bound form of the endonuclease domain exhibits higher endonuclease activity than the single-zinc-bound form. These results indicate that multiple zinc ions are required for the proper folding of the endonuclease domain, which would facilitate the endonuclease activity of aqMutL.
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Multiple zinc ions maintain the open conformation of the catalytic site in the DNA mismatch repair endonuclease MutL from Aquifex aeolicus.,Fukui K, Baba S, Kumasaka T, Yano T FEBS Lett. 2018 Apr 12. doi: 10.1002/1873-3468.13050. PMID:29645090<ref>PMID:29645090</ref>
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==See Also==
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*[[DNA mismatch repair protein 3D structures|DNA mismatch repair protein 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5z41" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Fukui, K]]
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[[Category: Aquifex aeolicus VF5]]
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[[Category: Yano, T]]
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[[Category: Large Structures]]
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[[Category: Dna binding protein]]
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[[Category: Fukui K]]
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[[Category: Endonuclease]]
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[[Category: Yano T]]
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[[Category: Mismatch repair protein]]
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[[Category: Thermophile]]
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[[Category: Zinc]]
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Current revision

Aquifex aeolicus MutL endonuclease domain with a single zinc ion.

PDB ID 5z41

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