5O8R

The crystal structure of DfoA bound to FAD and NADP; the desferrioxamine biosynthetic pathway cadaverine monooxygenase from the fire blight disease pathogen Erwinia amylovora

Summary for 5O8R

• Entry DOI: 10.2210/pdb5o8r/pdb
• Descriptor: L-lysine 6-monooxygenase involved in desferrioxamine biosynthesis, FLAVIN-ADENINE DINUCLEOTIDE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total)
• Functional Keywords: siderophore biosynthesis, cadaverine monooxygenase, nadp(h), fad, biosynthetic protein
• Biological source: Erwinia amylovora CFBP1430
• Total number of polymer chains: 2
• Total formula weight: 103917.30

Authors

Salomone-Stagni, M.,Bartho, J.D.,Polsinelli, I.,Bellini, D.,Walsh, M.A.,Demitri, N.,Benini, S. (deposition date: 2017-06-14, release date: 2018-02-28, Last modification date: 2024-05-08)

Primary citation

Salomone-Stagni, M.,Bartho, J.D.,Polsinelli, I.,Bellini, D.,Walsh, M.A.,Demitri, N.,Benini, S.
A complete structural characterization of the desferrioxamine E biosynthetic pathway from the fire blight pathogen Erwinia amylovora.
J. Struct. Biol., 202:236-249, 2018

PubMed Abstract: The Gram-negative bacterium Erwinia amylovora is the etiological agent of fire blight, a devastating disease which affects Rosaceae such as apple, pear and quince. The siderophore desferrioxamine E plays an important role in bacterial pathogenesis by scavenging iron from the host. DfoJ, DfoA and DfoC are the enzymes responsible for desferrioxamine production starting from lysine. We have determined the crystal structures of each enzyme in the desferrioxamine E pathway and demonstrate that the biosynthesis involves the concerted action of DfoJ, followed by DfoA and lastly DfoC. These data provide the first crystal structures of a Group II pyridoxal-dependent lysine decarboxylase, a cadaverine monooxygenase and a desferrioxamine synthetase. DfoJ is a homodimer made up of three domains. Each monomer contributes to the completion of the active site, which is positioned at the dimer interface. DfoA is the first structure of a cadaverine monooxygenase. It forms homotetramers whose subunits are built by two domains: one for FAD and one for NADP binding, the latter of which is formed by two subdomains. We propose a model for substrate binding and the role of residues 43-47 as gate keepers for FAD binding and the role of Arg97 in cofactors turnover. DfoC is the first structure of a desferrioxamine synthetase and the first of a multi-enzyme siderophore synthetase coupling an acyltransferase domain with a Non-Ribosomal Peptide Synthetase (NRPS)-Independent Siderophore domain (NIS).

PubMed: 29428557
DOI: 10.1016/j.jsb.2018.02.002

Experimental method

X-RAY DIFFRACTION (2.8 Å)