4IJJ

Structure of transcription factor DksA2 from Pseudomonas aeruginosa

Summary for 4IJJ

• Entry DOI: 10.2210/pdb4ijj/pdb
• Descriptor: Putative C4-type zinc finger protein, DksA/TraR family, SULFATE ION (3 entities in total)
• Functional Keywords: dksa fold, transcription factor, rna polymerase, disulfide bond, hydrolase
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 3
• Total formula weight: 48990.83

Authors

Biswas, T.,Furman, R.,Artsimovitch, I.,Tsodikov, O.V. (deposition date: 2012-12-21, release date: 2013-02-27, Last modification date: 2024-11-20)

Primary citation

Furman, R.,Biswas, T.,Danhart, E.M.,Foster, M.P.,Tsodikov, O.V.,Artsimovitch, I.
DksA2, a zinc-independent structural analog of the transcription factor DksA.
Febs Lett., 587:614-619, 2013

PubMed Abstract: Transcription factor DksA contains a four-Cys Zn(2 +)-finger motif thought to be responsible for structural integrity and the relative disposition of its domains. Pseudomonas aeruginosa encodes an additional DksA paralog (DksA2) that is expressed selectively under Zn(2+) limitation. Although DksA2 does not bind Zn(2+), it complements the Escherichia coli dksA deletion and has similar effects on transcription in vitro. In this study, structural and biochemical analyses reveal that DksA2 has a similar fold, domain structure and RNA polymerase binding properties to those of the E. coli DksA despite the lack of the stabilizing metal ion.

PubMed: 23416301
DOI: 10.1016/j.febslet.2013.01.073

Experimental method

X-RAY DIFFRACTION (3.25 Å)