The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
Crystal Structure of Rat DNA Polymerase β: Evidence for a Common Polymerase Mechanism
Abstract
Structures of the 31-kilodalton catalytic domain of rat DNA polymerase β (pol β) and the whole 39-kilodalton enzyme were determined at 2.3 and 3.6 angstrom resolution, respectively. The 31-kilodalton domain is composed of fingers, palm, and thumb subdomains arranged to form a DNA binding channel reminiscent of the polymerase domains of the Klenow fragment of Escherichia coli DNA polymerase I, HIV-1 reverse transcriptase, and bacteriophage T7 RNA polymerase. The amino-terminal 8-kilodalton domain is attached to the fingers subdomain by a flexible hinge. 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. The location of Mn 2+ and deoxyadenosine triphosphate in pol β confirms the role of the invariant aspartates in metal ion and deoxynucleoside triphosphate binding.
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Cited by
Recent Advances in Zinc Enzymology
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DNA Polymerases: Structural Diversity and Common Mechanisms
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Metadata
- Authors
- Sawaya, M. R., Pelletier, H., Kumar, A., Wilson, S. H., & Kraut, J.
- Venue
- Science
- Published
- 1994-06-24
- Volume
- 264
- Issue
- 5167
- Pages
- 1930-1935
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2166583656
- Cited by
- 469
- References
- 41
- FWCI
- 32.91
- Type
- journal article
- Language
- en
- Open access
- closed
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