1KU2

Crystal Structure of Thermus aquaticus RNA Polymerase Sigma Subunit Fragment Containing Regions 1.2 to 3.1

1KU2 の概要

• エントリーDOI: 10.2210/pdb1ku2/pdb
• 関連するPDBエントリー: 1ku3 1ku7
• 分子名称: sigma factor sigA, SULFATE ION (2 entities in total)
• 機能のキーワード: helices, transcription
• 由来する生物種: Thermus aquaticus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55421.90

構造登録者

Campbell, E.A.,Muzzin, O.,Chlenov, M.,Sun, J.L.,Olson, C.A.,Weinman, O.,Trester-Zedlitz, M.L.,Darst, S.A. (登録日: 2002-01-21, 公開日: 2002-04-03, 最終更新日: 2024-02-14)

主引用文献

Campbell, E.A.,Muzzin, O.,Chlenov, M.,Sun, J.L.,Olson, C.A.,Weinman, O.,Trester-Zedlitz, M.L.,Darst, S.A.
Structure of the bacterial RNA polymerase promoter specificity sigma subunit.
Mol.Cell, 9:527-539, 2002

PubMed Abstract: The sigma subunit is the key regulator of bacterial transcription. Proteolysis of Thermus aquaticus sigma(A), which occurred in situ during crystallization, reveals three domains, sigma(2), sigma(3), and sigma(4), connected by flexible linkers. Crystal structures of each domain were determined, as well as of sigma(4) complexed with -35 element DNA. Exposed surfaces of each domain are important for RNA polymerase binding. Universally conserved residues important for -10 element recognition and melting lie on one face of sigma(2), while residues important for extended -10 recognition lie on sigma(3). Genetic studies correctly predicted that a helix-turn-helix motif in sigma(4) recognizes the -35 element but not the details of the protein-DNA interactions. Positive control mutants in sigma(4) cluster in two regions, positioned to interact with activators bound just upstream or downstream of the -35 element.

PubMed: 11931761
DOI: 10.1016/S1097-2765(02)00470-7

実験手法

X-RAY DIFFRACTION (2.9 Å)