1FA0

STRUCTURE OF YEAST POLY(A) POLYMERASE BOUND TO MANGANATE AND 3'-DATP

1FA0 の概要

• エントリーDOI: 10.2210/pdb1fa0/pdb
• 分子名称: POLY(A)-POLYMERASE, MANGANESE (II) ION, 3'-DEOXYADENOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: polymerase, nucleotidyl transferase, transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Nucleus: P29468
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 124759.57

構造登録者

Bard, J.,Zhelkovsky, A.M.,Helmling, S.,Moore, C.L.,Bohm, A. (登録日: 2000-07-11, 公開日: 2000-08-30, 最終更新日: 2024-02-07)

主引用文献

Bard, J.,Zhelkovsky, A.M.,Helmling, S.,Earnest, T.N.,Moore, C.L.,Bohm, A.
Structure of yeast poly(A) polymerase alone and in complex with 3'-dATP.
Science, 289:1346-1349, 2000

PubMed Abstract: 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. The arrangement of these domains, however, is quite different from that seen in polymerases that use a template to select and position their incoming nucleotides. The first two domains are functionally analogous to polymerase palm and fingers domains. The third domain is attached to the fingers domain and is known to interact with the single-stranded RNA primer. In the nucleotide complex, two molecules of 3'-dATP are bound to Pap1. One occupies the position of the incoming base, prior to its addition to the mRNA chain. The other is believed to occupy the position of the 3' end of the mRNA primer.

PubMed: 10958780
DOI: 10.1126/science.289.5483.1346

実験手法

X-RAY DIFFRACTION (2.6 Å)