Amalendra Kumar

TL;DR: Two ternary complexes of rat DNA polymerase beta, a DNA template-primer, and dideoxycytidine triphosphate have been determined at 2.9 A and 3.6 A resolution, suggesting that the polymerase-DNA-ddCTP interactions are not affected by crystal packing forces.

TL;DR: The two invariant aspartates found in all polymerase sequences and implicated in catalytic activity have the same geometric arrangement within structurally similar but topologically distinct palms, indicating that the polymerases have maintained, or possibly re-evolved, a common nucleotidyl transfer mechanism.

TL;DR: Investigation of sequences surrounding the sites of methylation in A1 along with a compilation from the literature of sites that have been identified in other nuclear RNA binding proteins suggests a methylase-preferred recognition sequence of Phe/Gly-Gly/Phe, with the COOH-terminal flanking glycine being obligatory.

TL;DR: The lower fidelity observed with alanine mutants of Gly-262 and Trp-266 correlated with an over 200-fold increase in the dissociation rate constant for template-primer relative to wild type enzyme and suggests that enzyme-DNA interactions in the template-Primer stem are important fidelity determinants.

TL;DR: Alanine mutagenesis of αI lowered the apparent activity of every mutant relative to wild-type enzyme, and interactions between several residues of αH and the DNA minor groove, 3-5 nucleotides from the 3′-primer terminus, are suggested to be critical for DNA binding and fidelity.