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Overexpression, purification and crystallization of PhzA, the first enzyme of the phenazine biosynthesis pathway of Pseudomonas fluorescens 2-79.
- Source :
-
Acta crystallographica. Section D, Biological crystallography [Acta Crystallogr D Biol Crystallogr] 2004 Jun; Vol. 60 (Pt 6), pp. 1129-31. Date of Electronic Publication: 2004 May 21. - Publication Year :
- 2004
-
Abstract
- Phenazines are broad-spectrum antibiotic metabolites produced by organisms such as Pseudomonas and Streptomyces. Phenazines have been shown to enhance microbial competitiveness and the pathogenic potential of the organisms that synthesize them. PhzA (163 residues, approximate molecular weight 18.7 kDa) is the product of the first of seven genes of the operon responsible for phenazine biosynthesis in P. fluorescens 2-79. This enzyme is thought to catalyse one of the final steps in the formation of phenazine-1-carboxylic acid, the end product of phenazine biosynthesis in P. fluorescens 2-79. Here, the purification and crystallization of recombinant PhzA are reported. Crystals diffracting to 2.1 angstroms were obtained using 1.6 M magnesium sulfate and 2-morpholinoethanesulfonic acid monohydrate (MES) buffer pH 5.2-5.6. Crystals of both native and seleno-L-methionine-labelled protein belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 66.8, b = 75.3, c = 84.5 angstroms. The asymmetric unit contains one dimer of PhzA.<br /> (Copyright 2004 International Union of Crystallography)
- Subjects :
- Alkanesulfonic Acids chemistry
Crystallography, X-Ray
Dimerization
Hydrogen-Ion Concentration
Magnesium Sulfate pharmacology
Models, Chemical
Morpholines chemistry
Oligonucleotides chemistry
Protein Structure, Tertiary
Recombinant Proteins chemistry
Temperature
Enzymes chemistry
Phenazines chemistry
Pseudomonas fluorescens metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0907-4449
- Volume :
- 60
- Issue :
- Pt 6
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section D, Biological crystallography
- Publication Type :
- Academic Journal
- Accession number :
- 15159577
- Full Text :
- https://doi.org/10.1107/S090744490400767X