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| | <SX load='5m1s' size='340' side='right' viewer='molstar' caption='[[5m1s]], [[Resolution|resolution]] 6.70Å' scene=''> | | <SX load='5m1s' size='340' side='right' viewer='molstar' caption='[[5m1s]], [[Resolution|resolution]] 6.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5m1s]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M1S OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5M1S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5m1s]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M1S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5M1S FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dnaE, polC, b0184, JW0179 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), dnaN, b3701, JW3678 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), dnaQ, mutD, b0215, JW0205 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), holE, b1842, JW1831 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6.7Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </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=5m1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m1s OCA], [https://pdbe.org/5m1s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m1s RCSB], [https://www.ebi.ac.uk/pdbsum/5m1s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m1s ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5m1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m1s OCA], [http://pdbe.org/5m1s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m1s RCSB], [http://www.ebi.ac.uk/pdbsum/5m1s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m1s ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HOLE_ECOLI HOLE_ECOLI]] DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The exact function of the theta subunit is unknown. [[http://www.uniprot.org/uniprot/DPO3A_ECOLI DPO3A_ECOLI]] DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase. [[http://www.uniprot.org/uniprot/DPO3E_ECOLI DPO3E_ECOLI]] DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease. [[http://www.uniprot.org/uniprot/DPO3B_ECOLI DPO3B_ECOLI]] DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP-independent) along duplex DNA. | + | [https://www.uniprot.org/uniprot/DPO3A_ECOLI DPO3A_ECOLI] DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: DNA-directed DNA polymerase]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Ecoli]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Conrad, J]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Fernandez-Leiro, R]] | + | [[Category: Conrad J]] |
| - | [[Category: Lamers, M H]] | + | [[Category: Fernandez-Leiro R]] |
| - | [[Category: Scheres, S H.W]] | + | [[Category: Lamers MH]] |
| - | [[Category: Dna binding protein]]
| + | [[Category: Scheres SHW]] |
| - | [[Category: Dna editing proofreading exonuclease polymerase]]
| + | |
| Structural highlights
Function
DPO3A_ECOLI DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase.
Publication Abstract from PubMed
Faithful DNA replication is essential to all forms of life and depends on the action of 3'-5' exonucleases that remove misincorporated nucleotides from the newly synthesized strand. However, how the DNA is transferred from the polymerase to the exonuclease active site is not known. Here we present the cryo-EM structure of the editing mode of the catalytic core of the Escherichia coli replisome, revealing a dramatic distortion of the DNA whereby the polymerase thumb domain acts as a wedge that separates the two DNA strands. Importantly, NMR analysis of the DNA substrate shows that the presence of a mismatch increases the fraying of the DNA, thus enabling it to reach the exonuclease active site. Therefore the mismatch corrects itself, whereas the exonuclease subunit plays a passive role. Hence, our work provides unique insights into high-fidelity replication and establishes a new paradigm for the correction of misincorporated nucleotides.
Self-correcting mismatches during high-fidelity DNA replication.,Fernandez-Leiro R, Conrad J, Yang JC, Freund SM, Scheres SH, Lamers MH Nat Struct Mol Biol. 2017 Jan 9. doi: 10.1038/nsmb.3348. PMID:28067916[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fernandez-Leiro R, Conrad J, Yang JC, Freund SM, Scheres SH, Lamers MH. Self-correcting mismatches during high-fidelity DNA replication. Nat Struct Mol Biol. 2017 Jan 9. doi: 10.1038/nsmb.3348. PMID:28067916 doi:http://dx.doi.org/10.1038/nsmb.3348
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