3K4G

Crystal structure of E. coli RNA polymerase alpha subunit C-terminal domain

3K4G の概要

• エントリーDOI: 10.2210/pdb3k4g/pdb
• 分子名称: DNA-directed RNA polymerase subunit alpha, SODIUM ION (3 entities in total)
• 機能のキーワード: bacterial transcription regulation, dna-directed rna polymerase, nucleotidyltransferase, transcription, transferase
• 由来する生物種: Escherichia coli K-12
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 78391.02

構造登録者

Lara-Gonzalez, S.,Birktoft, J.,Lawson, C.L. (登録日: 2009-10-05, 公開日: 2010-07-07, 最終更新日: 2023-09-06)

主引用文献

Lara-Gonzalez, S.,Birktoft, J.J.,Lawson, C.L.
Structure of the Escherichia coli RNA polymerase alpha subunit C-terminal domain.
Acta Crystallogr.,Sect.D, 66:806-812, 2010

PubMed Abstract: The alpha subunit C-terminal domain (alphaCTD) of RNA polymerase (RNAP) is a key element in transcription activation in Escherichia coli, possessing determinants responsible for the interaction of RNAP with DNA and with transcription factors. Here, the crystal structure of E. coli alphaCTD (alpha subunit residues 245-329) determined to 2.0 A resolution is reported. Crystals were obtained after reductive methylation of the recombinantly expressed domain. The crystals belonged to space group P2(1) and possessed both pseudo-translational symmetry and pseudo-merohedral twinning. The refined coordinate model (R factor = 0.193, R(free) = 0.236) has improved geometry compared with prior lower resolution determinations of the alphaCTD structure [Jeon et al. (1995), Science, 270, 1495-1497; Benoff et al. (2002), Science, 297, 1562-1566]. An extensive dimerization interface formed primarily by N- and C-terminal residues is also observed. The new coordinates will facilitate the improved modeling of alphaCTD-containing multi-component complexes visualized at lower resolution using X-ray crystallography and electron-microscopy reconstruction.

PubMed: 20606261
DOI: 10.1107/S0907444910018470

実験手法

X-RAY DIFFRACTION (2.05 Å)