7RTY

Crystal Structure of PsfC from Pseudomonas syringae PB-5123

Summary for 7RTY

• Entry DOI: 10.2210/pdb7rty/pdb
• Descriptor: PsfC, FE (II) ION (3 entities in total)
• Functional Keywords: fosfomycin biosynthesis, metalloenzyme, fe, biosynthetic protein
• Biological source: Pseudomonas syringae
• Total number of polymer chains: 2
• Total formula weight: 54340.97

Authors

Ongpipattanakul, C.,Nair, S.K. (deposition date: 2021-08-16, release date: 2021-09-15, Last modification date: 2024-05-22)

Primary citation

Simon, M.A.,Ongpipattanakul, C.,Nair, S.K.,van der Donk, W.A.
Biosynthesis of fosfomycin in pseudomonads reveals an unexpected enzymatic activity in the metallohydrolase superfamily.
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed Abstract: The epoxide-containing phosphonate natural product fosfomycin is a broad-spectrum antibiotic used in the treatment of cystitis. Fosfomycin is produced by both the plant pathogen and soil-dwelling streptomycetes. While the streptomycete pathway has recently been fully elucidated, the pseudomonad pathway is still mostly elusive. Through a systematic evaluation of heterologous expression of putative biosynthetic enzymes, we identified the central enzyme responsible for completing the biosynthetic pathway in pseudomonads. The missing transformation involves the oxidative decarboxylation of the intermediate 2-phosphonomethylmalate to a new intermediate, 3-oxo-4-phosphonobutanoate, by PsfC. Crystallographic studies reveal that PsfC unexpectedly belongs to a new class of diiron metalloenzymes that are part of the polymerase and histidinol phosphatase superfamily.

PubMed: 34074759
DOI: 10.1073/pnas.2019863118

Experimental method

X-RAY DIFFRACTION (1.963 Å)