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6MU4

Bst DNA polymerase I FANA/DNA binary complex

Summary for 6MU4
Entry DOI10.2210/pdb6mu4/pdb
DescriptorDNA (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 Keywordsxna reverse transcription, transferase-dna complex, transferase/dna
Biological sourceGeobacillus stearothermophilus
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Total number of polymer chains3
Total formula weight74006.03
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 citationJackson, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.62 Å)
Structure validation

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