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3T22

Crystal structure of OxyR mutant from Porphyromonas gingivalis

Summary for 3T22
Entry DOI10.2210/pdb3t22/pdb
Related3HO7
DescriptorRedox-sensitive transcriptional activator OxyR (2 entities in total)
Functional Keywordsbeta-alpha-barrels, dna-binding, transcription regulation, transcription regulator
Biological sourcePorphyromonas gingivalis
Total number of polymer chains4
Total formula weight102422.04
Authors
Svintradze, D.V.,Wright, H.T.,Lewis, J.P. (deposition date: 2011-07-22, release date: 2013-04-17, Last modification date: 2023-09-13)
Primary citationSvintradze, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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