4fmo: Difference between revisions
New page: '''Unreleased structure''' The entry 4fmo is ON HOLD Authors: Charbonnier, JB Description: DNA repair protein complex |
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==Structure of the C-terminal domain of the Saccharomyces cerevisiae MUTL alpha (MLH1/PMS1) heterodimer bound to a fragment of exo1== | |||
<StructureSection load='4fmo' size='340' side='right'caption='[[4fmo]], [[Resolution|resolution]] 3.04Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4fmo]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FMO 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]] 3.04Å</td></tr> | |||
<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=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=4fmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fmo OCA], [https://pdbe.org/4fmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fmo RCSB], [https://www.ebi.ac.uk/pdbsum/4fmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fmo ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MLH1_YEAST MLH1_YEAST] Required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. Component of different MutL heterodimers that form a ternary complex with the MutS heterodimers, which initially recognize the DNA mismatches. This complex is thought to be responsible for directing the downsteam MMR events, including strand discrimination, excision, and resynthesis. Plays a major role in maintaining the genetic stability of simple sequence repeats, the repair of heteroduplex sites present in meiotic recombination intermediates, and the promotion of meiotic crossing-over.<ref>PMID:9545323</ref> <ref>PMID:10570173</ref> <ref>PMID:12529393</ref> | |||
==See Also== | |||
*[[DNA mismatch repair protein 3D structures|DNA mismatch repair protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae S288C]] | |||
[[Category: Charbonnier JB]] | |||
[[Category: Gueneau E]] | |||
[[Category: Legrand P]] |
Latest revision as of 18:29, 14 March 2024
Structure of the C-terminal domain of the Saccharomyces cerevisiae MUTL alpha (MLH1/PMS1) heterodimer bound to a fragment of exo1Structure of the C-terminal domain of the Saccharomyces cerevisiae MUTL alpha (MLH1/PMS1) heterodimer bound to a fragment of exo1
Structural highlights
FunctionMLH1_YEAST Required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops (IDLs) resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. Component of different MutL heterodimers that form a ternary complex with the MutS heterodimers, which initially recognize the DNA mismatches. This complex is thought to be responsible for directing the downsteam MMR events, including strand discrimination, excision, and resynthesis. Plays a major role in maintaining the genetic stability of simple sequence repeats, the repair of heteroduplex sites present in meiotic recombination intermediates, and the promotion of meiotic crossing-over.[1] [2] [3] See AlsoReferences
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