3UKI

Crystal structure of reduced OxyR from Porphyromonas gingivalis

3UKI の概要

• エントリーDOI: 10.2210/pdb3uki/pdb
• 関連するPDBエントリー: 3HO7 3T22
• 分子名称: OxyR (1 entity in total)
• 機能のキーワード: beta-alpha-barrels, dna-binding, transcription regulation, redox-sensitive transcription regulation, transcription regulator
• 由来する生物種: Porphyromonas gingivalis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 102486.30

構造登録者

Svintradze, D.V.,Wright, H.T.,Collazo-Santiago, E.A.,Lewis, J.P. (登録日: 2011-11-09, 公開日: 2013-07-31, 最終更新日: 2023-09-13)

主引用文献

Svintradze, D.V.,Peterson, D.L.,Collazo-Santiago, E.A.,Lewis, J.P.,Wright, H.T.
Structures of the Porphyromonas gingivalis OxyR regulatory domain explain differences in expression of the OxyR regulon in Escherichia coli and P. gingivalis.
Acta Crystallogr.,Sect.D, 69:2091-2103, 2013

PubMed Abstract: OxyR transcriptionally regulates Escherichia coli oxidative stress response genes through a reversibly reducible cysteine disulfide biosensor of cellular redox status. Structural changes induced by redox changes in these cysteines are conformationally transmitted to the dimer subunit interfaces, which alters dimer and tetramer interactions with DNA. In contrast to E. coli OxyR regulatory-domain structures, crystal structures of Porphyromonas gingivalis OxyR regulatory domains show minimal differences in dimer configuration on changes in cysteine disulfide redox status. This locked configuration of the P. gingivalis OxyR regulatory-domain dimer closely resembles the oxidized (activating) form of the E. coli OxyR regulatory-domain dimer. It correlates with the observed constitutive activation of some oxidative stress genes in P. gingivalis and is attributable to a single amino-acid insertion in P. gingivalis OxyR relative to E. coli OxyR. Modelling of full-length P. gingivalis, E. coli and Neisseria meningitidis OxyR-DNA complexes predicts different modes of DNA binding for the reduced and oxidized forms of each.

PubMed: 24100327
DOI: 10.1107/S0907444913019471

実験手法

X-RAY DIFFRACTION (4.15 Å)