5akb: Difference between revisions
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==MutS in complex with the N-terminal domain of MutL - crystal form 1== | |||
<StructureSection load='5akb' size='340' side='right'caption='[[5akb]], [[Resolution|resolution]] 4.71Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5akb]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AKB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AKB 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]] 4.71Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</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=5akb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5akb OCA], [https://pdbe.org/5akb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5akb RCSB], [https://www.ebi.ac.uk/pdbsum/5akb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5akb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MUTS_ECOLI MUTS_ECOLI] This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
To avoid mutations in the genome, DNA replication is generally followed by DNA mismatch repair (MMR). MMR starts when a MutS homolog recognizes a mismatch and undergoes an ATP-dependent transformation to an elusive sliding clamp state. How this transient state promotes MutL homolog recruitment and activation of repair is unclear. Here we present a crystal structure of the MutS/MutL complex using a site-specifically crosslinked complex and examine how large conformational changes lead to activation of MutL. The structure captures MutS in the sliding clamp conformation, where tilting of the MutS subunits across each other pushes DNA into a new channel, and reorientation of the connector domain creates an interface for MutL with both MutS subunits. Our work explains how the sliding clamp promotes loading of MutL onto DNA, to activate downstream effectors. We thus elucidate a crucial mechanism that ensures that MMR is initiated only after detection of a DNA mismatch. | |||
MutS/MutL crystal structure reveals that the MutS sliding clamp loads MutL onto DNA.,Groothuizen FS, Winkler I, Cristovao M, Fish A, Winterwerp HH, Reumer A, Marx AD, Hermans N, Nicholls RA, Murshudov GN, Lebbink JH, Friedhoff P, Sixma TK Elife. 2015 Jul 11;4. doi: 10.7554/eLife.06744. PMID:26163658<ref>PMID:26163658</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5akb" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[DNA mismatch repair protein 3D structures|DNA mismatch repair protein 3D structures]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli K-12]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Cristovao M]] | ||
[[Category: | [[Category: Fish A]] | ||
[[Category: Winterwerp | [[Category: Friedhoff P]] | ||
[[Category: Groothuizen FS]] | |||
[[Category: Hermans N]] | |||
[[Category: Lebbink JHG]] | |||
[[Category: Marx AD]] | |||
[[Category: Murshudov GN]] | |||
[[Category: Nicholls RA]] | |||
[[Category: Reumer A]] | |||
[[Category: Sixma TK]] | |||
[[Category: Winkler I]] | |||
[[Category: Winterwerp HHK]] | |||
Latest revision as of 14:11, 10 January 2024
MutS in complex with the N-terminal domain of MutL - crystal form 1MutS in complex with the N-terminal domain of MutL - crystal form 1
Structural highlights
FunctionMUTS_ECOLI This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. Publication Abstract from PubMedTo avoid mutations in the genome, DNA replication is generally followed by DNA mismatch repair (MMR). MMR starts when a MutS homolog recognizes a mismatch and undergoes an ATP-dependent transformation to an elusive sliding clamp state. How this transient state promotes MutL homolog recruitment and activation of repair is unclear. Here we present a crystal structure of the MutS/MutL complex using a site-specifically crosslinked complex and examine how large conformational changes lead to activation of MutL. The structure captures MutS in the sliding clamp conformation, where tilting of the MutS subunits across each other pushes DNA into a new channel, and reorientation of the connector domain creates an interface for MutL with both MutS subunits. Our work explains how the sliding clamp promotes loading of MutL onto DNA, to activate downstream effectors. We thus elucidate a crucial mechanism that ensures that MMR is initiated only after detection of a DNA mismatch. MutS/MutL crystal structure reveals that the MutS sliding clamp loads MutL onto DNA.,Groothuizen FS, Winkler I, Cristovao M, Fish A, Winterwerp HH, Reumer A, Marx AD, Hermans N, Nicholls RA, Murshudov GN, Lebbink JH, Friedhoff P, Sixma TK Elife. 2015 Jul 11;4. doi: 10.7554/eLife.06744. PMID:26163658[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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