6cul

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

spinqualitylabelsall models 6cul, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6cul is a 8 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: CIT, FGD, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9I184_PSEAE Publication Abstract from PubMed The hydroxyornithine transformylase from Pseudomonas aeruginosa is known by the gene name pvdF, and has been hypothesized to use N(10)-formyltetrahydrofolate (N(10)-fTHF) as a co-substrate formyl donor to convert N(5)-hydroxyornithine (OHOrn) to N(5)-formyl- N(5)-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 2.3A, revealing a formyltransferase fold consistent with N(10)-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. PvdF of pyoverdin biosynthesis is a structurally unique N(10)-formyltetrahydrofolate-dependent formyltransferase.,Kenjic N, Hoag MR, Moraski GC, Caperelli CA, Moran GR, Lamb AL Arch Biochem Biophys. 2019 Jan 26;664:40-50. doi: 10.1016/j.abb.2019.01.028. PMID:30689984 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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