PDBsum entry 3ho7

Transcription

PDB id: 3ho7

Contents

Protein chains

220 a.a. *

Waters ×418

* Residue conservation analysis

PDB id:

3ho7

Name:

Transcription

Title:

Crystal structure of oxyr from porphyromonas gingivalis

Structure:

Oxyr. Chain: a, b. Fragment: regulatory domain. Synonym: redox-sensitive transcriptional activator oxyr. Engineered: yes

Source:

Porphyromonas gingivalis. Bacteroides gingivalis. Organism_taxid: 837. Strain: atcc 33277 / dsm 20709 / jcm 12257. Gene: oxyr, pg_0270. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.58Å R-factor: 0.220 R-free: 0.245

Authors:

D.V.Svintradze,H.T.Wright,J.P.Lewis

Key ref:

D.V.Svintradze et al. (2013). Structures of the Porphyromonas gingivalis OxyR regulatory domain explain differences in expression of the OxyR regulon in Escherichia coli and P. gingivalis. Acta Crystallogr D Biol Crystallogr, 69, 2091-2103. PubMed id: 24100327 DOI: 10.1107/S0907444913019471

Date:

01-Jun-09 Release date: 09-Jun-10

Protein chains

Q7MXD3  (Q7MXD3_PORGI) -  Redox-sensitive transcriptional activator OxyR from Porphyromonas gingivalis (strain ATCC BAA-308 / W83)

Seq: 308 a.a.

Struc: 220 a.a.

DOI no: 10.1107/S0907444913019471

Acta Crystallogr D Biol Crystallogr 69:2091-2103 (2013)

PubMed id: 24100327

Structures of the Porphyromonas gingivalis OxyR regulatory domain explain differences in expression of the OxyR regulon in Escherichia coli and P. gingivalis.

D.V.Svintradze, D.L.Peterson, E.A.Collazo-Santiago, J.P.Lewis, H.T.Wright.

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.