6CUL
PvdF of pyoverdin biosynthesis is a structurally unique N10-formyltetrahydrofolate-dependent formyltransferase
6CUL の概要
| エントリーDOI | 10.2210/pdb6cul/pdb |
| 分子名称 | 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) |
| 機能のキーワード | n10-formyltetrahydrofolate-dependent formyltransferase, transferase |
| 由来する生物種 | Pseudomonas aeruginosa PAO1 |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 254721.97 |
| 構造登録者 | Kenjic, N.,Hoag, M.R.,Moraski, G.C.,Caperelli, C.A.,Moran, G.R.,Lamb, A.L. (登録日: 2018-03-26, 公開日: 2019-02-06, 最終更新日: 2024-11-20) |
| 主引用文献 | 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 Cited by 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: 30689984DOI: 10.1016/j.abb.2019.01.028 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.3 Å) |
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