1BDF

STRUCTURE OF ESCHERICHIA COLI RNA POLYMERASE ALPHA SUBUNIT N-TERMINAL DOMAIN

1BDF の概要

• エントリーDOI: 10.2210/pdb1bdf/pdb
• 分子名称: RNA POLYMERASE ALPHA SUBUNIT (2 entities in total)
• 機能のキーワード: nucleotidyltransferase, rnap, alpha, assemble
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 103653.97

構造登録者

Zhang, G.,Darst, S.A. (登録日: 1998-05-08, 公開日: 1999-05-11, 最終更新日: 2024-02-07)

主引用文献

Zhang, G.,Darst, S.A.
Structure of the Escherichia coli RNA polymerase alpha subunit amino-terminal domain.
Science, 281:262-266, 1998

PubMed Abstract: The 2.5 angstrom resolution x-ray crystal structure of the Escherichia coli RNA polymerase (RNAP) alpha subunit amino-terminal domain (alphaNTD), which is necessary and sufficient to dimerize and assemble the other RNAP subunits into a transcriptionally active enzyme and contains all of the sequence elements conserved among eukaryotic alpha homologs, has been determined. The alphaNTD monomer comprises two distinct, flexibly linked domains, only one of which participates in the dimer interface. In the alphaNTD dimer, a pair of helices from one monomer interact with the cognate helices of the other to form an extensive hydrophobic core. All of the determinants for interactions with the other RNAP subunits lie on one face of the alphaNTD dimer. Sequence alignments, combined with secondary-structure predictions, support proposals that a heterodimer of the eukaryotic RNAP subunits related to Saccharomyces cerevisiae Rpb3 and Rpb11 plays the role of the alphaNTD dimer in prokaryotic RNAP.

PubMed: 9657722
DOI: 10.1126/science.281.5374.262

実験手法

X-RAY DIFFRACTION (2.5 Å)