5x9w
From Proteopedia
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<StructureSection load='5x9w' size='340' side='right' caption='[[5x9w]], [[Resolution|resolution]] 3.30Å' scene=''> | <StructureSection load='5x9w' size='340' side='right' caption='[[5x9w]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5x9w]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X9W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X9W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5x9w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Neig1 Neig1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X9W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X9W FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mutS, NGO1930 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=242231 NEIG1])</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=5x9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x9w OCA], [http://pdbe.org/5x9w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x9w RCSB], [http://www.ebi.ac.uk/pdbsum/5x9w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x9w ProSAT]</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=5x9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x9w OCA], [http://pdbe.org/5x9w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x9w RCSB], [http://www.ebi.ac.uk/pdbsum/5x9w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x9w ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/MUTS_NEIG1 MUTS_NEIG1]] 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. | [[http://www.uniprot.org/uniprot/MUTS_NEIG1 MUTS_NEIG1]] 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 == | ||
| + | The DNA mismatch repair (MMR) pathway removes errors that appear during genome replication. MutS is the primary mismatch sensor and forms an asymmetric dimer that encircles DNA to bend it to scan for mismatches. The mechanism utilized to load DNA into the central tunnel was unknown and the origin of the force required to bend DNA was unclear. We show that, in absence of DNA, MutS forms a symmetric dimer wherein a gap exists between the monomers through which DNA can enter the central tunnel. The comparison with structures of MutS-DNA complexes suggests that the mismatch scanning monomer (Bm) will move by nearly 50 A to associate with the other monomer (Am). Consequently, the N-terminal domains of both monomers will press onto DNA to bend it. The proposed mechanism of toroid formation evinces that the force required to bend DNA arises primarily due to the movement of Bm and hence, the MutS dimer acts like a pair of pliers to bend DNA. We also shed light on the allosteric mechanism that influences the expulsion of adenosine triphosphate from Am on DNA binding. Overall, this study provides mechanistic insight regarding the primary event in MMR i.e. the assembly of the MutS-DNA complex. | ||
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| + | Mechanism of formation of a toroid around DNA by the mismatch sensor protein.,Nirwal S, Kulkarni DS, Sharma A, Rao DN, Nair DT Nucleic Acids Res. 2017 Nov 22. pii: 4647669. doi: 10.1093/nar/gkx1149. PMID:29182773<ref>PMID:29182773</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5x9w" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Neig1]] | ||
[[Category: Nair, D T]] | [[Category: Nair, D T]] | ||
[[Category: Nirwal, S]] | [[Category: Nirwal, S]] | ||
Revision as of 07:36, 13 December 2017
Mismatch Repair Protein
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