7ou0: Difference between revisions
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==The structure of MutS bound to two molecules of ADP-Vanadate== | ==The structure of MutS bound to two molecules of ADP-Vanadate== | ||
<StructureSection load='7ou0' size='340' side='right'caption='[[7ou0]]' scene=''> | <StructureSection load='7ou0' size='340' side='right'caption='[[7ou0]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OU0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7ou0]] is a 2 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=7OU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OU0 FirstGlance]. <br> | ||
</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=7ou0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ou0 OCA], [https://pdbe.org/7ou0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ou0 RCSB], [https://www.ebi.ac.uk/pdbsum/7ou0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ou0 ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</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=7ou0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ou0 OCA], [https://pdbe.org/7ou0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ou0 RCSB], [https://www.ebi.ac.uk/pdbsum/7ou0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ou0 ProSAT]</span></td></tr> | |||
</table> | </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 == | |||
DNA mismatch repair detects and corrects mismatches introduced during DNA replication. The protein MutS scans for mismatches and coordinates the repair cascade. During this process, MutS undergoes multiple conformational changes in response to ATP binding, hydrolysis and release, but how ATP induces the various MutS conformations is incompletely understood. Here we present four cryogenic electron microscopy structures of Escherichia coli MutS at sequential stages of the ATP hydrolysis cycle that reveal how ATP binding and hydrolysis induce closing and opening of the MutS dimer, respectively. Biophysical analysis demonstrates how DNA binding modulates the ATPase cycle by prevention of hydrolysis during scanning and mismatch binding, while preventing ADP release in the sliding clamp state. Nucleotide release is achieved when MutS encounters single-stranded DNA that is produced during removal of the daughter strand. The combination of ATP binding and hydrolysis and its modulation by DNA enables MutS to adopt the different conformations needed to coordinate the sequential steps of the mismatch repair cascade. | |||
Cryogenic electron microscopy structures reveal how ATP and DNA binding in MutS coordinates sequential steps of DNA mismatch repair.,Borsellini A, Kunetsky V, Friedhoff P, Lamers MH Nat Struct Mol Biol. 2022 Jan;29(1):59-66. doi: 10.1038/s41594-021-00707-1. Epub , 2022 Jan 10. PMID:35013597<ref>PMID:35013597</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7ou0" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[DNA mismatch repair protein 3D structures|DNA mismatch repair protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Borsellini A]] | [[Category: Borsellini A]] | ||
Revision as of 09:23, 26 October 2022
The structure of MutS bound to two molecules of ADP-VanadateThe structure of MutS bound to two molecules of ADP-Vanadate
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 PubMedDNA mismatch repair detects and corrects mismatches introduced during DNA replication. The protein MutS scans for mismatches and coordinates the repair cascade. During this process, MutS undergoes multiple conformational changes in response to ATP binding, hydrolysis and release, but how ATP induces the various MutS conformations is incompletely understood. Here we present four cryogenic electron microscopy structures of Escherichia coli MutS at sequential stages of the ATP hydrolysis cycle that reveal how ATP binding and hydrolysis induce closing and opening of the MutS dimer, respectively. Biophysical analysis demonstrates how DNA binding modulates the ATPase cycle by prevention of hydrolysis during scanning and mismatch binding, while preventing ADP release in the sliding clamp state. Nucleotide release is achieved when MutS encounters single-stranded DNA that is produced during removal of the daughter strand. The combination of ATP binding and hydrolysis and its modulation by DNA enables MutS to adopt the different conformations needed to coordinate the sequential steps of the mismatch repair cascade. Cryogenic electron microscopy structures reveal how ATP and DNA binding in MutS coordinates sequential steps of DNA mismatch repair.,Borsellini A, Kunetsky V, Friedhoff P, Lamers MH Nat Struct Mol Biol. 2022 Jan;29(1):59-66. doi: 10.1038/s41594-021-00707-1. Epub , 2022 Jan 10. PMID:35013597[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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