Crystal Structure of PhzD protein from Pseudomonas aeruginosaCrystal Structure of PhzD protein from Pseudomonas aeruginosa

Structural highlights

1nf9 is a 1 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PHZD1_PSEAE Involved in the biosynthesis of the antibiotic phenazine, a nitrogen-containing heterocyclic molecule. PhzD1 (operon phzA1B1C1E1F1G1) has a role in the biosynthesis of the phenazine during planktonic growth (PubMed:23129634). Catalyzes the hydrolysis of the vinyl ether functional group of 2-amino-2-deoxyisochorismate (ADIC), yielding pyruvate and trans-2,3-dihydro-3-hydroxyanthranilic acid (DHHA) (PubMed:12741825, PubMed:23129634). Also able to act on isochorismate, chorismate and 4-amino-4-deoxychorismate (ADC) as substrates (PubMed:12741825).[1] [2] [3]

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. Parsons JF, Calabrese K, Eisenstein E, Ladner JE. Structure and mechanism of Pseudomonas aeruginosa PhzD, an isochorismatase from the phenazine biosynthetic pathway. Biochemistry. 2003 May 20;42(19):5684-93. PMID:12741825 doi:10.1021/bi027385d
  2. Recinos DA, Sekedat MD, Hernandez A, Cohen TS, Sakhtah H, Prince AS, Price-Whelan A, Dietrich LE. Redundant phenazine operons in Pseudomonas aeruginosa exhibit environment-dependent expression and differential roles in pathogenicity. Proc Natl Acad Sci U S A. 2012 Nov 20;109(47):19420-5. PMID:23129634 doi:10.1073/pnas.1213901109
  3. Mavrodi DV, Bonsall RF, Delaney SM, Soule MJ, Phillips G, Thomashow LS. Functional analysis of genes for biosynthesis of pyocyanin and phenazine-1-carboxamide from Pseudomonas aeruginosa PAO1. J Bacteriol. 2001 Nov;183(21):6454-65. PMID:11591691 doi:10.1128/JB.183.21.6454-6465.2001

1nf9, resolution 1.50Å

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