6CUL

PvdF of pyoverdin biosynthesis is a structurally unique N10-formyltetrahydrofolate-dependent formyltransferase

Summary for 6CUL

• Entry DOI: 10.2210/pdb6cul/pdb
• Descriptor: Pyoverdine synthetase F, N-(4-{[(2-amino-4-oxo-1,4-dihydroquinazolin-6-yl)methyl]amino}benzene-1-carbonyl)-D-glutamic acid, CITRIC ACID, ... (4 entities in total)
• Functional Keywords: n10-formyltetrahydrofolate-dependent formyltransferase, transferase
• Biological source: Pseudomonas aeruginosa PAO1
• Total number of polymer chains: 8
• Total formula weight: 254721.97

Authors

Kenjic, N.,Hoag, M.R.,Moraski, G.C.,Caperelli, C.A.,Moran, G.R.,Lamb, A.L. (deposition date: 2018-03-26, release date: 2019-02-06, Last modification date: 2024-11-20)

Primary citation

Kenjic, N.,Hoag, M.R.,Moraski, G.C.,Caperelli, C.A.,Moran, G.R.,Lamb, A.L.
PvdF of pyoverdin biosynthesis is a structurally unique N10-formyltetrahydrofolate-dependent formyltransferase.
Arch. Biochem. Biophys., 664:40-50, 2019

PubMed Abstract: The hydroxyornithine transformylase from Pseudomonas aeruginosa is known by the gene name pvdF, and has been hypothesized to use N-formyltetrahydrofolate (N-fTHF) as a co-substrate formyl donor to convert N-hydroxyornithine (OHOrn) to N-formyl- N-hydroxyornithine (fOHOrn). PvdF is in the biosynthetic pathway for pyoverdin biosynthesis, a siderophore generated under iron-limiting conditions that has been linked to virulence, quorum sensing and biofilm formation. The structure of PvdF was determined by X-ray crystallography to 2.3 Å, revealing a formyltransferase fold consistent with N-formyltetrahydrofolate dependent enzymes, such as the glycinamide ribonucleotide transformylases, N-sugar transformylases and methionyl-tRNA transformylases. Whereas the core structure, including the catalytic triad, is conserved, PvdF has three insertions of 18 or more amino acids, which we hypothesize are key to binding the OHOrn substrate. Steady state kinetics revealed a non-hyperbolic rate curve, promoting the hypothesis that PvdF uses a random-sequential mechanism, and favors folate binding over OHOrn.

PubMed: 30689984
DOI: 10.1016/j.abb.2019.01.028

Experimental method

X-RAY DIFFRACTION (2.3 Å)