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| ==Bacillus DNA Polymerase I Large Fragment complex 7== | | ==Bacillus DNA Polymerase I Large Fragment complex 7== |
| <StructureSection load='4f8r' size='340' side='right' caption='[[4f8r]], [[Resolution|resolution]] 1.64Å' scene=''> | | <StructureSection load='4f8r' size='340' side='right'caption='[[4f8r]], [[Resolution|resolution]] 1.64Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4f8r]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Geoka Geoka]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F8R OCA]. <br> | | <table><tr><td colspan='2'>[[4f8r]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_kaustophilus_HTA426 Geobacillus kaustophilus HTA426] 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=4F8R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F8R FirstGlance]. <br> |
| </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><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]] 1.64Å</td></tr> |
| <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DDG:2,3-DIDEOXY-GUANOSINE-5-MONOPHOSPHATE'>DDG</scene></td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DDG:2,3-DIDEOXY-GUANOSINE-5-MONOPHOSPHATE'>DDG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ez6|4ez6]], [[4ez9|4ez9]], [[4f3o|4f3o]], [[4f4k|4f4k]], [[4f2r|4f2r]], [[4f2s|4f2s]]</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=4f8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f8r OCA], [https://pdbe.org/4f8r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f8r RCSB], [https://www.ebi.ac.uk/pdbsum/4f8r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f8r ProSAT]</span></td></tr> |
| <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">polA, GK2730 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=235909 GEOKA])</td></tr> | | </table> |
| <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
| | == Function == |
| <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4f8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f8r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f8r RCSB], [http://www.ebi.ac.uk/pdbsum/4f8r PDBsum]</span></td></tr>
| | [https://www.uniprot.org/uniprot/Q5KWC1_GEOKA Q5KWC1_GEOKA] |
| <table> | |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed == | |
| Even though high-fidelity polymerases copy DNA with remarkable accuracy, some base-pair mismatches are incorporated at low frequency, leading to spontaneous mutagenesis. Using high-resolution X-ray crystallographic analysis of a DNA polymerase that catalyzes replication in crystals, we observe that a C*A mismatch can mimic the shape of cognate base pairs at the site of incorporation. This shape mimicry enables the mismatch to evade the error detection mechanisms of the polymerase, which would normally either prevent mismatch incorporation or promote its nucleolytic excision. Movement of a single proton on one of the mismatched bases alters the hydrogen-bonding pattern such that a base pair forms with an overall shape that is virtually indistinguishable from a canonical, Watson-Crick base pair in double-stranded DNA. These observations provide structural evidence for the rare tautomer hypothesis of spontaneous mutagenesis, a long-standing concept that has been difficult to demonstrate directly.
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| Structural evidence for the rare tautomer hypothesis of spontaneous mutagenesis.,Wang W, Hellinga HW, Beese LS Proc Natl Acad Sci U S A. 2011 Oct 25;108(43):17644-8. Epub 2011 Oct 17. PMID:22006298<ref>PMID:22006298</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| | ==See Also== |
| </div>
| | *[[DNA polymerase 3D structures|DNA polymerase 3D structures]] |
| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: DNA-directed DNA polymerase]] | | [[Category: Geobacillus kaustophilus HTA426]] |
| [[Category: Geoka]] | | [[Category: Large Structures]] |
| [[Category: Beese, L S.]] | | [[Category: Synthetic construct]] |
| [[Category: Wang, W.]] | | [[Category: Beese LS]] |
| [[Category: Closed form]] | | [[Category: Wang W]] |
| [[Category: Dna polymerase i]]
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| [[Category: Transferase-dna complex]]
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