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Article

Structure of yeast poly(A) polymerase alone and in complex with 3'-dATP.

Science (New York, N.Y.) - 25 Aug 2000

Bard J, Zhelkovsky A M, Helmling S, Earnest T N, Moore C L, Bohm A

Abstract excerpt

Polyadenylate [poly(A)] polymerase (PAP) catalyzes the addition of a polyadenosine tail to almost all eukaryotic messenger RNAs (mRNAs). The crystal structure of the PAP from Saccharomyces cerevisiae (Pap1) has been solved to 2.6 angstroms, both alone and in complex with 3'-deoxyadenosine triphosphate (3'-dATP). Like other nucleic acid polymerases, Pap1 is composed of three domains that encircle the active site....

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Identifiers

PMID: 10958780
DOI: 10.1126/science.289.5483.1346

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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