6MU4

Bst DNA polymerase I FANA/DNA binary complex

Summary for 6MU4

• Entry DOI: 10.2210/pdb6mu4/pdb
• Descriptor: DNA (5'-D(P*GP*CP*GP*AP*TP*CP*AP*CP*GP*T)-3'), DNA polymerase I, FANA (5'-D(P*(UF2)P*(A5L)P*(CFL)P*(GFL)P*(UF2)P*(GFL)P*(A5L)P*(UF2)P*(CFL)P*(GFL)P*(CFL))-3'), ... (7 entities in total)
• Functional Keywords: xna reverse transcription, transferase-dna complex, transferase/dna
• Biological source: Geobacillus stearothermophilus; More
• Total number of polymer chains: 3
• Total formula weight: 74006.03

Authors

Jackson, L.N.,Chim, N.,Chaput, J.C. (deposition date: 2018-10-22, release date: 2019-06-05, Last modification date: 2023-10-11)

Primary citation

Jackson, L.N.,Chim, N.,Shi, C.,Chaput, J.C.
Crystal structures of a natural DNA polymerase that functions as an XNA reverse transcriptase.
Nucleic Acids Res., 47:6973-6983, 2019

PubMed Abstract: 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-β-d-arabino nucleic acid (FANA) and α-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.

PubMed: 31170294
DOI: 10.1093/nar/gkz513

Experimental method

X-RAY DIFFRACTION (1.62 Å)