3JV9

The structure of a reduced form of OxyR from N. meningitidis

Summary for 3JV9

• Entry DOI: 10.2210/pdb3jv9/pdb
• Descriptor: Transcriptional regulator, LysR family, CHLORIDE ION (3 entities in total)
• Functional Keywords: lysr-type transcriptional regulator, lttr, redox, structural genomics, oppf, oxford protein production facility, dna-binding, transcription, transcription regulation, oppf3291
• Biological source: Neisseria meningitidis
• Total number of polymer chains: 2
• Total formula weight: 49257.53

Authors

Sainsbury, S.,Ren, J.,Stuart, D.I.,Owens, R.J.,Oxford Protein Production Facility (OPPF) (deposition date: 2009-09-16, release date: 2010-06-16, Last modification date: 2024-11-20)

Primary citation

Sainsbury, S.,Ren, J.,Nettleship, J.E.,Saunders, N.J.,Stuart, D.I.,Owens, R.J.
The structure of a reduced form of OxyR from Neisseria meningitidis
Bmc Struct.Biol., 10:10-10, 2010

PubMed Abstract: Survival of the human pathogen, Neisseria meningitidis, requires an effective response to oxidative stress resulting from the release of hydrogen peroxide by cells of the human immune system. In N. meningitidis, expression of catalase, which is responsible for detoxifying hydrogen peroxide, is controlled by OxyR, a redox responsive LysR-type regulator. OxyR responds directly to intracellular hydrogen peroxide through the reversible formation of a disulphide bond between C199 and C208 in the regulatory domain of the protein.

PubMed: 20478059
DOI: 10.1186/1472-6807-10-10

Experimental method

X-RAY DIFFRACTION (2.39 Å)