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<StructureSection load='6mu5' size='340' side='right'caption='[[6mu5]], [[Resolution|resolution]] 1.91Å' scene=''> | <StructureSection load='6mu5' size='340' side='right'caption='[[6mu5]], [[Resolution|resolution]] 1.91Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6mu5]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MU5 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6mu5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] 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=6MU5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MU5 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.912Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FA2:5-(6-AMINO-9H-PURIN-9-YL)-4-HYDROXYTETRAHYDROFURAN-3-YL+DIHYDROGEN+PHOSPHATE'>FA2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TC:4-[5-[[3-[(CYCLOPROPYLAMINO)METHYL]PHENYL]AMINO]-1H-PYRAZOL-3-YL]-[1,1-BIPHENYL]-2,4-DIOL'>TC</scene>, <scene name='pdbligand=TFT:(L)-ALPHA-THREOFURANOSYL-THYMINE-3-MONOPHOSPHATE'>TFT</scene>, <scene name='pdbligand=TG:(2S,4R)-1-(3-AMINO-2-METHYLBENZOYL)-4-HYDROXY-N-(4-(4-METHYLTHIAZOL-5-YL)BENZYL)PYRROLIDINE-2-CARBOXAMIDE'>TG</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=6mu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mu5 OCA], [https://pdbe.org/6mu5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mu5 RCSB], [https://www.ebi.ac.uk/pdbsum/6mu5 PDBsum], [https://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'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/E1C9K5_GEOSE E1C9K5_GEOSE] | |||
<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> | ||
[[Category: | [[Category: Geobacillus stearothermophilus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: | [[Category: Chaput JC]] | ||
[[Category: | [[Category: Chim N]] | ||
[[Category: | [[Category: Jackson LN]] | ||
Latest revision as of 09:38, 11 October 2023
Bst DNA polymerase I TNA/DNA binary complexBst DNA polymerase I TNA/DNA binary complex
Structural highlights
FunctionPublication Abstract from PubMedReplicative 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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