3DKW

Crystal Structure of DNR from Pseudomonas aeruginosa.

Summary for 3DKW

• Entry DOI: 10.2210/pdb3dkw/pdb
• Related: 2Z69
• Descriptor: DNR protein (1 entity in total)
• Functional Keywords: crp-fnr, hth, beta barrel, dimerization helix, homodimer, transcription regulator
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 10
• Total formula weight: 259658.03

Authors

Giardina, G. (deposition date: 2008-06-26, release date: 2009-05-19, Last modification date: 2023-11-01)

Primary citation

Giardina, G.,Rinaldo, S.,Castiglione, N.,Caruso, M.,Cutruzzola, F.
A dramatic conformational rearrangement is necessary for the activation of DNR from Pseudomonas aeruginosa. Crystal structure of wild-type DNR.
Proteins, 2009

PubMed Abstract: The opportunistic pathogen Pseudomonas aeruginosa can grow in low oxygen, because it is capable of anaerobic respiration using nitrate as a terminal electron acceptor (denitrification). An intermediate of the denitrification pathway is nitric oxide, a compound that may become cytotoxic at high concentration. The intracellular levels of nitric oxide are tightly controlled by regulating the expression of the enzymes responsible for its synthesis and degradation (nitrite and nitric oxide reductases). In this article, we present the crystallographic structure of the wild-type dissimilative nitrate respiration regulator (DNR), a master regulator controlling expression of the denitrification machinery and a putative target for new therapeutic strategies. Comparison with other structures among the CRP-FNR class of regulators reveals that DNR has crystallized in a conformation that has never been observed before. In particular, the sensing domain of DNR has undergone a rotation of more than 50 degrees with respect to the other structures. This suggests that DNR may undergo an unexpected and very large conformational rearrangement on activation.

PubMed: 19415759
DOI: 10.1002/prot.22428

Experimental method

X-RAY DIFFRACTION (3.6 Å)