4fmo - Revision history

OCA at 15:29, 14 March 2024

2024-03-14T15:29:07Z

← Older revision		Revision as of 15:29, 14 March 2024
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	== Structural highlights ==		== 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>		<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='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>		</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>		<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>		</table>
	== Function ==		== 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>		[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>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Mismatch-repair factors have a prominent role in surveying eukaryotic DNA-replication fidelity and in ensuring correct meiotic recombination. These functions depend on MutL-homolog heterodimers with Mlh1. In humans, MLH1 mutations underlie half of hereditary nonpolyposis colorectal cancers (HNPCCs). Here we report crystal structures of the MutLalpha (Mlh1-Pms1 heterodimer) C-terminal domain (CTD) from Saccharomyces cerevisiae, alone and in complex with fragments derived from Mlh1 partners. These structures reveal structural rearrangements and additional domains in MutLalpha as compared to the bacterial MutL counterparts and show that the strictly conserved C terminus of Mlh1 forms part of the Pms1 endonuclease site. The structures of the ternary complexes between MutLalpha(CTD) and Exo1 or Ntg2 fragments reveal the binding mode of the MIP-box motif shared by several Mlh1 partners. Finally, the structures provide a rationale for the deleterious impact of MLH1 mutations in HNPCCs.

	Structure of the MutLalpha C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site.,Gueneau E, Dherin C, Legrand P, Tellier-Lebegue C, Gilquin B, Bonnesoeur P, Londino F, Quemener C, Le Du MH, Marquez JA, Moutiez M, Gondry M, Boiteux S, Charbonnier JB Nat Struct Mol Biol. 2013 Apr;20(4):461-8. doi: 10.1038/nsmb.2511. Epub 2013 Feb , 24. PMID:23435383<ref>PMID:23435383</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4fmo" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==

OCA at 19:58, 19 October 2022

2022-10-19T19:58:58Z

← Older revision		Revision as of 19:58, 19 October 2022
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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==		==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=''>		<StructureSection load='4fmo' size='340' side='right'caption='[[4fmo]], [[Resolution\|resolution]] 3.04Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4fmo]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Baker's_yeast Baker's yeast~~]. 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 [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4FMO FirstGlance]. <br>		<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='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>~~</td></tr>~~		</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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fmn\|4fmn]], [[4e4w\|4e4w]]</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>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MLH1, PMS2, YMR167W, YM8520.16 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), PMS1, YNL082W, N2317 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=4fmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fmo OCA], [~~http~~://pdbe.org/4fmo PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4fmo RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4fmo PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4fmo ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://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> [[http://www.uniprot.org/uniprot/EXO1_YEAST EXO1_YEAST]] 5'->3' double-stranded DNA exonuclease involved in mismatch repair and eventually also in mitotic recombination between direct repeats. Also has a minor role in the correction of large DNA mismatches that occur in the heteroduplex DNA during meiotic recombination at the HIS4 locus.<ref>PMID:9207118</ref> <ref>PMID:9111347</ref> <ref>PMID:11102356</ref> <ref>PMID:15629726</ref> [[http://www.uniprot.org/uniprot/PMS1_YEAST PMS1_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 the MutLalpha heterodimer that forms 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 and in the repair of heteroduplex sites present in meiotic recombination intermediates.<ref>PMID:9545323</ref> <ref>PMID:10570173</ref> <ref>PMID:16227575</ref>		[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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 4fmo" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4fmo" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[DNA mismatch repair protein 3D structures\|DNA mismatch repair protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Baker's yeast~~]]		[[Category: Large Structures]]
	[[Category: ~~Charbonnier, J B~~]]		[[Category: Saccharomyces cerevisiae S288C]]
	[[Category: ~~Gueneau, E~~]]		[[Category: Charbonnier JB]]
	[[Category: ~~Legrand, P~~]]		[[Category: Gueneau E]]
	[[Category: ~~Dna damage]]~~		[[Category: Legrand P]]
	~~[[Category: Dna repair]]~~
	~~[[Category: Endonuclease]]~~
	~~[[Category: Hydrolase]]~~
	~~[[Category: Mismatch repair]]~~
	~~[[Category: Mutl]]~~
	~~[[Category: Zn-binding protein~~]]

OCA at 10:03, 5 August 2016

2016-08-05T10:03:28Z

← Older revision		Revision as of 10:03, 5 August 2016
Line 1:		Line 1:

	==Structure of the C-terminal domain of the Saccharomyces cerevisiae MUTL alpha (MLH1/PMS1) heterodimer bound to a fragment of exo1==		==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=''>		<StructureSection load='4fmo' size='340' side='right' caption='[[4fmo]], [[Resolution\|resolution]] 3.04Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4fmo]] is a 3 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FMO FirstGlance]. <br>		<table><tr><td colspan='2'>[[4fmo]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FMO FirstGlance]. <br>
	</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=ZN:ZINC+ION'>ZN</scene></td></tr>		</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=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fmn\|4fmn]], [[4e4w\|4e4w]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fmn\|4fmn]], [[4e4w\|4e4w]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MLH1, PMS2, YMR167W, YM8520.16 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 ~~Saccharomyces cerevisiae S288c~~]), PMS1, YNL082W, N2317 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 ~~Saccharomyces cerevisiae S288c~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MLH1, PMS2, YMR167W, YM8520.16 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), PMS1, YNL082W, N2317 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=4fmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fmo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fmo RCSB], [http://www.ebi.ac.uk/pdbsum/4fmo 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=4fmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fmo OCA], [http://pdbe.org/4fmo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fmo RCSB], [http://www.ebi.ac.uk/pdbsum/4fmo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fmo ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 4fmo" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Saccharomyces cerevisiae s288c~~]]		[[Category: Baker's yeast]]
	[[Category: Charbonnier, J B]]		[[Category: Charbonnier, J B]]
	[[Category: Gueneau, E]]		[[Category: Gueneau, E]]

OCA at 17:54, 25 December 2014

2014-12-25T17:54:29Z

← Older revision		Revision as of 17:54, 25 December 2014
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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=4fmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fmo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fmo RCSB], [http://www.ebi.ac.uk/pdbsum/4fmo 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=4fmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fmo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fmo RCSB], [http://www.ebi.ac.uk/pdbsum/4fmo PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://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> [[http://www.uniprot.org/uniprot/EXO1_YEAST EXO1_YEAST]] 5'->3' double-stranded DNA exonuclease involved in mismatch repair and eventually also in mitotic recombination between direct repeats. Also has a minor role in the correction of large DNA mismatches that occur in the heteroduplex DNA during meiotic recombination at the HIS4 locus.<ref>PMID:9207118</ref> <ref>PMID:9111347</ref> <ref>PMID:11102356</ref> <ref>PMID:15629726</ref> [[http://www.uniprot.org/uniprot/PMS1_YEAST PMS1_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 the MutLalpha heterodimer that forms 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 and in the repair of heteroduplex sites present in meiotic recombination intermediates.<ref>PMID:9545323</ref> <ref>PMID:10570173</ref> <ref>PMID:16227575</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 11:31, 21 December 2014

2014-12-21T11:31:31Z

← Older revision		Revision as of 11:31, 21 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_4fmo\| PDB=4fmo \| SCENE= }}~~		==Structure of the C-terminal domain of the Saccharomyces cerevisiae MUTL alpha (MLH1/PMS1) heterodimer bound to a fragment of exo1==
	===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=''>
	~~{{ABSTRACT_PUBMED_23435383}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[4fmo]] is a 3 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FMO FirstGlance]. <br>
			</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=ZN:ZINC+ION'>ZN</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4fmn\|4fmn]], [[4e4w\|4e4w]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MLH1, PMS2, YMR167W, YM8520.16 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c]), PMS1, YNL082W, N2317 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</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=4fmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fmo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fmo RCSB], [http://www.ebi.ac.uk/pdbsum/4fmo PDBsum]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Mismatch-repair factors have a prominent role in surveying eukaryotic DNA-replication fidelity and in ensuring correct meiotic recombination. These functions depend on MutL-homolog heterodimers with Mlh1. In humans, MLH1 mutations underlie half of hereditary nonpolyposis colorectal cancers (HNPCCs). Here we report crystal structures of the MutLalpha (Mlh1-Pms1 heterodimer) C-terminal domain (CTD) from Saccharomyces cerevisiae, alone and in complex with fragments derived from Mlh1 partners. These structures reveal structural rearrangements and additional domains in MutLalpha as compared to the bacterial MutL counterparts and show that the strictly conserved C terminus of Mlh1 forms part of the Pms1 endonuclease site. The structures of the ternary complexes between MutLalpha(CTD) and Exo1 or Ntg2 fragments reveal the binding mode of the MIP-box motif shared by several Mlh1 partners. Finally, the structures provide a rationale for the deleterious impact of MLH1 mutations in HNPCCs.

	~~==Function==~~		Structure of the MutLalpha C-terminal domain reveals how Mlh1 contributes to Pms1 endonuclease site.,Gueneau E, Dherin C, Legrand P, Tellier-Lebegue C, Gilquin B, Bonnesoeur P, Londino F, Quemener C, Le Du MH, Marquez JA, Moutiez M, Gondry M, Boiteux S, Charbonnier JB Nat Struct Mol Biol. 2013 Apr;20(4):461-8. doi: 10.1038/nsmb.2511. Epub 2013 Feb , 24. PMID:23435383<ref>PMID:23435383</ref>
	~~[[http://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> [[http~~:~~//www.uniprot.org/uniprot/EXO1_YEAST EXO1_YEAST]] 5'->3' double~~-stranded DNA exonuclease involved in mismatch repair and eventually also in mitotic recombination between direct repeats. Also has a minor role in the correction of large DNA mismatches that occur in the heteroduplex DNA during meiotic recombination at the HIS4 locus.~~<ref>PMID:9207118</ref> <ref>PMID:9111347</ref> <ref>PMID:11102356</ref> <ref>PMID:15629726</ref> [[http~~:~~//www~~.~~uniprot.org/uniprot~~/PMS1_YEAST PMS1_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 the MutLalpha heterodimer that forms 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 and in the repair of heteroduplex sites present in meiotic recombination intermediates.~~<ref>PMID:9545323</ref> <ref>~~PMID:~~10570173</ref>~~ <ref>PMID:~~16227575~~</ref>

	~~==About this Structure==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[4fmo]] is~~ a ~~3 chain structure with sequence from [http://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].~~		</div>
			== References ==
	==~~Reference~~==		<references/>
	~~<ref group="xtra">PMID:023435383</ref>~~<references ~~group="xtra"~~/><~~references~~/>		__TOC__
			</StructureSection>
	[[Category: Saccharomyces cerevisiae s288c]]		[[Category: Saccharomyces cerevisiae s288c]]
	[[Category: Charbonnier, J B.]]		[[Category: Charbonnier, J B]]
	[[Category: Gueneau, E.]]		[[Category: Gueneau, E]]
	[[Category: Legrand, P.]]		[[Category: Legrand, P]]
	[[Category: Dna damage]]		[[Category: Dna damage]]
	[[Category: Dna repair]]		[[Category: Dna repair]]

OCA at 05:18, 28 August 2013

2013-08-28T05:18:42Z

← Older revision		Revision as of 05:18, 28 August 2013
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	~~[[Image:4fmo.jpg\|left\|200px]]~~

	{{STRUCTURE_4fmo\| PDB=4fmo \| SCENE= }}		{{STRUCTURE_4fmo\| PDB=4fmo \| SCENE= }}

	===Structure of the C-terminal domain of the Saccharomyces cerevisiae MUTL alpha (MLH1/PMS1) heterodimer bound to a fragment of exo1===		===Structure of the C-terminal domain of the Saccharomyces cerevisiae MUTL alpha (MLH1/PMS1) heterodimer bound to a fragment of exo1===
			{{ABSTRACT_PUBMED_23435383}}

			==Function==
			[[http://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> [[http://www.uniprot.org/uniprot/EXO1_YEAST EXO1_YEAST]] 5'->3' double-stranded DNA exonuclease involved in mismatch repair and eventually also in mitotic recombination between direct repeats. Also has a minor role in the correction of large DNA mismatches that occur in the heteroduplex DNA during meiotic recombination at the HIS4 locus.<ref>PMID:9207118</ref> <ref>PMID:9111347</ref> <ref>PMID:11102356</ref> <ref>PMID:15629726</ref> [[http://www.uniprot.org/uniprot/PMS1_YEAST PMS1_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 the MutLalpha heterodimer that forms 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 and in the repair of heteroduplex sites present in meiotic recombination intermediates.<ref>PMID:9545323</ref> <ref>PMID:10570173</ref> <ref>PMID:16227575</ref>

	==About this Structure==		==About this Structure==
	[[4fmo]] is a 3 chain structure with sequence from [http://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].		[[4fmo]] is a 3 chain structure with sequence from [http://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].

			==Reference==
			<ref group="xtra">PMID:023435383</ref><references group="xtra"/><references/>
	[[Category: Saccharomyces cerevisiae s288c]]		[[Category: Saccharomyces cerevisiae s288c]]
	[[Category: Charbonnier, J B.]]		[[Category: Charbonnier, J B.]]

OCA at 13:57, 20 February 2013

2013-02-20T13:57:20Z

← Older revision		Revision as of 13:57, 20 February 2013
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	~~'''Unreleased structure'''~~		[[Image:4fmo.jpg\|left\|200px]]

	~~The entry~~ 4fmo ~~is ON HOLD~~ ~~until Paper Publication~~		{{STRUCTURE_4fmo\| PDB=4fmo \| SCENE= }}

	~~Authors: Gueneau, E., Legrand, P., Charbonnier, J.B.~~		===Structure of the C-terminal domain of the Saccharomyces cerevisiae MUTL alpha (MLH1/PMS1) heterodimer bound to a fragment of exo1===

	~~Description~~: ~~Structure of the C~~-~~terminal domain of the~~ Saccharomyces cerevisiae ~~MUTL alpha (MLH1/PMS1) heterodimer bound to a fragment of exo1~~
			==About this Structure==
			[[4fmo]] is a 3 chain structure with sequence from [http://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].
			[[Category: Saccharomyces cerevisiae s288c]]
			[[Category: Charbonnier, J B.]]
			[[Category: Gueneau, E.]]
			[[Category: Legrand, P.]]
			[[Category: Dna damage]]
			[[Category: Dna repair]]
			[[Category: Endonuclease]]
			[[Category: Hydrolase]]
			[[Category: Mismatch repair]]
			[[Category: Mutl]]
			[[Category: Zn-binding protein]]

OCA at 08:15, 16 January 2013

2013-01-16T08:15:55Z

← Older revision		Revision as of 08:15, 16 January 2013
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	The entry 4fmo is ON HOLD until Paper Publication		The entry 4fmo is ON HOLD until Paper Publication

	Authors: Charbonnier, JB		Authors: Gueneau, E., Legrand, P., Charbonnier, J.B.

	Description: ~~DNA repair protein complex~~		Description: Structure of the C-terminal domain of the Saccharomyces cerevisiae MUTL alpha (MLH1/PMS1) heterodimer bound to a fragment of exo1

OCA at 13:16, 8 November 2012

2012-11-08T13:16:27Z

← Older revision		Revision as of 13:16, 8 November 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4fmo is ON HOLD		The entry 4fmo is ON HOLD until Paper Publication

	Authors: Charbonnier, JB		Authors: Charbonnier, JB

	Description: DNA repair protein complex		Description: DNA repair protein complex

OCA: Protected "4fmo" [edit=sysop:move=sysop]

2012-06-27T05:27:02Z

Protected "4fmo" [edit=sysop:move=sysop]

← Older revision	Revision as of 05:27, 27 June 2012
(No difference)