6EYV

Crystal structure of the pyoverdine maturation protein PvdP in complex with the mock substrates L-tyrosine and zinc.

6EYV の概要

• エントリーDOI: 10.2210/pdb6eyv/pdb
• 関連するPDBエントリー: 6EYS
• 分子名称: PvdP, ZINC ION, TYROSINE, ... (4 entities in total)
• 機能のキーワード: tyrosinase, pyoverdine, barrel, zinc, oxidoreductase
• 由来する生物種: Pseudomonas aeruginosa (strain UCBPP-PA14)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 124140.28

構造登録者

Poppe, J.,Blankenfeldt, W. (登録日: 2017-11-13, 公開日: 2018-08-01, 最終更新日: 2024-01-17)

主引用文献

Poppe, J.,Reichelt, J.,Blankenfeldt, W.
Pseudomonas aeruginosapyoverdine maturation enzyme PvdP has a noncanonical domain architecture and affords insight into a new subclass of tyrosinases.
J. Biol. Chem., 293:14926-14936, 2018

PubMed Abstract: Pyoverdines (PVDs) are important chromophore-containing siderophores of fluorescent pseudomonad bacteria such as the opportunistic human pathogen in which they play an essential role in host infection. PVD biosynthesis encompasses a complex pathway comprising cytosolic nonribosomal peptide synthetases that produce a polypeptide precursor that periplasmic enzymes convert to the final product. The structures of most enzymes involved in PVD chromophore maturation have been elucidated, but the structure of the essential tyrosinase PvdP, a monooxygenase required for the penultimate step in PVD biosynthesis, is not known. Here, we closed this gap by determining the crystal structure of PvdP in an apo and tyrosine-complexed state at 2.1 and 2.7 Å, respectively. These structures revealed that PvdP is a homodimer, with each chain consisting of a C-terminal tyrosinase domain and an N-terminal eight-stranded β-barrel reminiscent of streptavidin that appears to have a structural role only. We observed that ligand binding leads to the displacement of a "placeholder" tyrosine that blocks the active site in the apo structure. This exposes a large, deep binding site that seems suitable for accommodating ferribactin, a substrate of PvdP in PVD biosynthesis. The binding site consists almost exclusively of residues from the tyrosinase domain. Of note, we also found that this domain is more closely related to tyrosinases from arthropods rather than to tyrosinases from other bacteria. In conclusion, our work unravels the structural basis of PvdP's activity in PVD biosynthesis, observations that may inform structure-guided development of PvdP-specific inhibitors to manage infections.

PubMed: 30030378
DOI: 10.1074/jbc.RA118.002560

実験手法

X-RAY DIFFRACTION (2.704 Å)