5EZ7

Crystal structure of the FAD dependent oxidoreductase PA4991 from Pseudomonas aeruginosa

Summary for 5EZ7

• Entry DOI: 10.2210/pdb5ez7/pdb
• Descriptor: flavoenzyme PA4991, FLAVIN-ADENINE DINUCLEOTIDE, MERCURY (II) ION, ... (4 entities in total)
• Functional Keywords: flavoenzyme, flavine, oxidoreductase
• Biological source: Pseudomonas aeruginosa PAO1
• Total number of polymer chains: 1
• Total formula weight: 43438.10

Authors

Jacewicz, A.,Schnell, R.,Lindqvist, Y.,Schneider, G. (deposition date: 2015-11-26, release date: 2016-02-17, Last modification date: 2024-05-01)

Primary citation

Jacewicz, A.,Schnell, R.,Lindqvist, Y.,Schneider, G.
Crystal structure of the flavoenzyme PA4991 from Pseudomonas aeruginosa.
Acta Crystallogr.,Sect.F, 72:105-111, 2016

PubMed Abstract: The locus PA4991 in Pseudomonas aeruginosa encodes an open reading frame that has been identified as essential for the virulence and/or survival of this pathogenic organism in the infected host. Here, it is shown that this gene encodes a monomeric FAD-binding protein of molecular mass 42.2 kDa. The structure of PA4991 was determined by a combination of molecular replacement using a search model generated with Rosetta and phase improvement by a low-occupancy heavy-metal derivative. PA4991 belongs to the GR2 family of FAD-dependent oxidoreductases, comprising an FAD-binding domain typical of the glutathione reductase family and a second domain dominated by an eight-stranded mixed β-sheet. Most of the protein-FAD interactions are via the FAD-binding domain, but the isoalloxazine ring is located at the domain interface and interacts with residues from both domains. A comparison with the structurally related glycine oxidase and glycerol-3-phosphate dehydrogenase shows that in spite of very low amino-acid sequence identity (<18%) several active-site residues involved in substrate binding in these enzymes are conserved in PA4991. However, enzymatic assays show that PA4991 does not display amino-acid oxidase or glycerol-3-phosphate dehydrogenase activities, suggesting that it requires different substrates for activity.

PubMed: 26841760
DOI: 10.1107/S2053230X15024437

Experimental method

X-RAY DIFFRACTION (2.4 Å)