43 Antibody

1. Co(2+) and Mn(2+) enhanced ground-state binding of both correct and incorrect dNTPs to RB69pol:dideoxy-terminated primer-template complexes. PMID: 27096230
2. Data indicate that alanine replacement of residues distant from the active site of the replicative RB69 DNA polymerase renders the enzyme incapable of sustaining phage replication in vivo. PMID: 24116139
3. structures of the various RB69pol ternary complexes can be used to rationalize the results obtained from pre-steady-state kinetic assays[review] PMID: 24720884
4. Determined is the crystal structure of the dATP/tC(o)-containing ternary complex of the RB69 DNA polymerase Y567A mutant at 1.9 A resolution; the incoming dATP formed two hydrogen bonds with an imino-tautomerized form of tC(o). PMID: 22616982
5. evaluated the contribution of minor groove hydrogen bonding interactions with RB69pol PMID: 22571765
6. The miscoding potential of 5-hydroxycytosine arises due to template instability in the DNA polymerase active site. PMID: 22026756
7. The authors show that the S565G/Y567A mutant generally had greater base selectivity than the Y567A mutant and that the kinetic parameters for dNMP insertion, excision of the 3'-terminal nucleotide residue, and primer extension beyond a mispair differed. PMID: 21216248
8. The structure of an RB69 pol ternary complex at 1.8 A is reported. A network of five highly ordered, buried water molecules can be seen to interact with the N3 and O2 atoms in the minor groove of the DNA duplex. PMID: 21158418
9. When Y567A and S565G replacements were combined, mutator activity was strongly decreased compared to that with Y567A replacement alone. PMID: 20950625
10. Data describe the crystal structures of the pol alpha family RB69 DNA polymerase with DNA containing the two most prevalent, spontaneously generated premutagenic lesions PMID: 15057282
11. Results describe the structure of the bacteriophage RB69 replicative DNA polymerase attempting to process an abasic site analog. PMID: 15057283
12. The Y619F substitution would disrupt the hydrogen bond network at the primer terminus and may affect the alignment of the 3' primer terminus at the polymerase active site, slowing chemistry and overall DNA synthesis. PMID: 17321543
13. Binding of a metal ion to the A site is required for the nucleotidyl transfer reaction, but is insufficient to initiate the enzyme isomerization. Binding of a dNTP, in the absence of a metal ion, is sufficient to induce this conformational change. PMID: 19228036
14. The effect of A and B metal ion site occupancy on the rates of Fingers closing and on the affinity of Rh.dTTP for the E.D binary complex of the catalytic site of RB69 DNA polymerase was studied. PMID: 19228037

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KEGG: vg:1494172