Crystal Structure of Rat DNA Polymerase β: Evidence for a Common Polymerase Mechanism

• DOI: 10.1126/science.7516581
• Publication Date: 2006-10-06T00:01:25Z
• Authors: Michael R. Sawaya; Huguette Pelletier; Amalendra Kumar; Samuel H. Wilson; Joseph Kraut
• Keywords: DNA clamp; DNA polymerase I; Klenow fragment; DNA polymerase II; DNA polymerase beta; Processivity; DNA polymerase mu

Structures of the 31-kilodalton catalytic domain rat DNA polymerase β (pol β) and whole 39-kilodalton enzyme were determined at 2.3 3.6 angstrom resolution, respectively. The is composed fingers, palm, thumb subdomains arranged to form a binding channel reminiscent domains Klenow fragment Escherichia coli I, HIV-1 reverse transcriptase, bacteriophage T7 RNA polymerase. amino-terminal 8-kilodalton attached fingers subdomain by flexible hinge. two invariant aspartates found in all sequences implicated activity have same geometric arrangement within structurally similar but topologically distinct palms, indicating that polymerases maintained, or possibly re-evolved, common nucleotidyl transfer mechanism. location Mn 2+ deoxyadenosine triphosphate pol confirms role metal ion deoxynucleoside binding.