3E59
Crystal structure of the PvcA (PA2254) protein from Pseudomonas aeruginosa
Summary for 3E59
| Entry DOI | 10.2210/pdb3e59/pdb |
| Descriptor | Pyoverdine biosynthesis protein PvcA, PHOSPHATE ION, TRIETHYLENE GLYCOL, ... (4 entities in total) |
| Functional Keywords | pvca, isonitrile, paerucumarin, 2-isocyano-6, 7-dihydroxycoumarin, transferase |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 4 |
| Total formula weight | 150384.76 |
| Authors | Gulick, A.M.,Drake, E.J. (deposition date: 2008-08-13, release date: 2008-10-14, Last modification date: 2024-02-21) |
| Primary citation | Drake, E.J.,Gulick, A.M. Three-dimensional structures of Pseudomonas aeruginosa PvcA and PvcB, two proteins involved in the synthesis of 2-isocyano-6,7-dihydroxycoumarin. J.Mol.Biol., 384:193-205, 2008 Cited by PubMed Abstract: The pvcABCD operon of Pseudomonas aeruginosa encodes four proteins (PA2254, PA2255, PA2256, and PA2257) that form a cluster that is responsible for the synthesis of a cyclized isocyano derivative of tyrosine. These proteins, which were identified originally as being responsible for a step in the maturation of the chromophore of the peptide siderophore pyoverdine, have been identified recently as belonging to a family of proteins that produce small organic isonitriles. We report that strains harboring a disruption in the pvcA or pvcB genes are able to grow in iron-depleted conditions and to produce pyoverdine. Additionally, we have determined the three-dimensional crystal structures of PvcA and PvcB. The structure of PvcA demonstrates a novel enzyme architecture that is built upon a Rossmann fold. We have analyzed the sequence conservation of enzymes within this family and identified six conserved motifs. These regions of the protein cluster around a putative active site cavity. The structure of the PvcB protein confirms it is a member of the Fe2+/alpha-ketoglutarate-dependent oxygenase family of enzymes. The active site of PvcB is compared to the structures of other family members and suggests that a conformational change to order several loops will accompany the binding of ligands. PubMed: 18824174DOI: 10.1016/j.jmb.2008.09.027 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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