PDBsum entry 5o7t

Transferase

PDB id: 5o7t

Contents

Protein chain

540 a.a.

DNA/RNA

Ligands

DCP

GOL

Metals

_MG ×3

Waters ×265

PDB id:

5o7t

Name:

Transferase

Title:

Crystal structure of klentaq mutant m747k in a closed ternary complex with a dg:dctp base pair

Structure:

DNA polymerase i, thermostable. Chain: a. Synonym: taq polymerase 1. Engineered: yes. Mutation: yes. DNA primer. Chain: b. Engineered: yes. DNA template.

Source:

Thermus aquaticus. Organism_taxid: 271. Gene: pola, pol1. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Synthetic construct. Organism_taxid: 32630. Organism_taxid: 32630

Resolution:

1.80Å R-factor: 0.180 R-free: 0.235

Authors:

K.Betz,K.Diederichs,A.Marx

Key ref:

K.Betz et al. (2017). Structural basis for the selective incorporation of an artificial nucleotide opposite a DNA adduct by a DNA polymerase. Chem Commun (Camb), 53, 12704-12707. PubMed id: 29136072 DOI: 10.1039/c7cc07173f

Date:

09-Jun-17 Release date: 29-Nov-17

Protein chain

P19821  (DPO1_THEAQ) -  DNA polymerase I, thermostable from Thermus aquaticus

Seq: 832 a.a.

Struc: 540 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DNA/RNA chains

G-A-C-C-A-C-G-G-C-G-C-DDG 12 bases

A-A-A-G-C-G-C-G-C-C-G-T-G-G-T-C 16 bases

Enzyme reactions

• Enzyme class: E.C.2.7.7.7 - DNA-directed Dna polymerase.
• Reaction: DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1039/c7cc07173f

Chem Commun (Camb) 53:12704-12707 (2017)

PubMed id: 29136072

Structural basis for the selective incorporation of an artificial nucleotide opposite a DNA adduct by a DNA polymerase.

K.Betz, A.Nilforoushan, L.A.Wyss, K.Diederichs, S.J.Sturla, A.Marx.

ABSTRACT

The possibility to sequence cytotoxic O⁶-alkylG DNA adducts would greatly benefit research. Recently we reported a benzimidazole-derived nucleotide that is selectively incorporated opposite the damaged site by a mutated DNA polymerase. Here we provide the structural basis for this reaction which may spur future developments in DNA damage sequencing.