5E41

Crystal structure of the large fragment of DNA Polymerase I from Thermus aquaticus in a closed ternary complex with 5-(N-(10-hydroxydecanoyl)-aminopentenyl)-2'-deoxyuridine-triphosphate

Summary for 5E41

• Entry DOI: 10.2210/pdb5e41/pdb
• Descriptor: DNA polymerase I, thermostable, DNA (5'-D(*GP*AP*CP*CP*AP*CP*GP*GP*CP*GP*CP*(DOC))-3'), DNA (5'-D(*AP*AP*AP*AP*GP*GP*CP*GP*CP*CP*GP*TP*GP*GP*TP*C)-3'), ... (7 entities in total)
• Functional Keywords: linker-modified nucleotide, klentaq, dna polymerase, transferase
• Biological source: Thermus aquaticus; More
• Total number of polymer chains: 3
• Total formula weight: 70641.06

Authors

Hottin, A.,Betz, K.,Marx, A. (deposition date: 2015-10-05, release date: 2016-12-07, Last modification date: 2024-01-10)

Primary citation

Hottin, A.,Betz, K.,Diederichs, K.,Marx, A.
Structural Basis for the KlenTaq DNA Polymerase Catalysed Incorporation of Alkene- versus Alkyne-Modified Nucleotides.
Chemistry, 23:2109-2118, 2017

PubMed Abstract: Efficient incorporation of modified nucleotides by DNA polymerases is essential for many cutting-edge biomolecular technologies. The present study compares the acceptance of either alkene- or alkyne-modified nucleotides by KlenTaq DNA polymerase and provides structural insights into how 7-deaza-adenosine and deoxyuridine with attached alkene-modifications are incorporated into the growing DNA strand. Thereby, we identified modified nucleotides that prove to be superior substrates for KlenTaq DNA polymerase compared with their natural analogues. The knowledge can be used to guide future design of functionalized nucleotide building blocks.

PubMed: 27901305
DOI: 10.1002/chem.201604515

Experimental method

X-RAY DIFFRACTION (1.8 Å)