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6mu5
From Proteopedia
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<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=6mu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mu5 OCA], [http://pdbe.org/6mu5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mu5 RCSB], [http://www.ebi.ac.uk/pdbsum/6mu5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mu5 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=6mu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mu5 OCA], [http://pdbe.org/6mu5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mu5 RCSB], [http://www.ebi.ac.uk/pdbsum/6mu5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mu5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Replicative DNA polymerases are highly efficient enzymes that maintain stringent geometric control over shape and orientation of the template and incoming nucleoside triphosphate. In a surprising twist to this paradigm, a naturally occurring bacterial DNA polymerase I member isolated from Geobacillus stearothermophilus (Bst) exhibits an innate ability to reverse transcribe RNA and other synthetic congeners (XNAs) into DNA. This observation raises the interesting question of how a replicative DNA polymerase is able to recognize templates of diverse chemical composition. Here, we present crystal structures of natural Bst DNA polymerase that capture the post-translocated product of DNA synthesis on templates composed entirely of 2'-deoxy-2'-fluoro-beta-d-arabino nucleic acid (FANA) and alpha-l-threofuranosyl nucleic acid (TNA). Analysis of the enzyme active site reveals the importance of structural plasticity as a possible mechanism for XNA-dependent DNA synthesis and provides insights into the construction of variants with improved activity. | ||
| + | |||
| + | Crystal structures of a natural DNA polymerase that functions as an XNA reverse transcriptase.,Jackson LN, Chim N, Shi C, Chaput JC Nucleic Acids Res. 2019 Jun 6. pii: 5512092. doi: 10.1093/nar/gkz513. PMID:31170294<ref>PMID:31170294</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6mu5" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[DNA polymerase 3D structures|DNA polymerase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:32, 19 June 2019
Bst DNA polymerase I TNA/DNA binary complex
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