7XLZ

Structure of siderophore-interacting protein from Vibrio anguillarum

7XLZ の概要

• エントリーDOI: 10.2210/pdb7xlz/pdb
• 分子名称: Siderophore-interacting protein, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: siderophore-interacting protein, iron release, vibrio anguillarum, oxidoreductase
• 由来する生物種: Vibrio anguillarum (strain ATCC 68554 / 775) (Listonella anguillarum)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61674.52

構造登録者

Ma, Q.,Liu, C.,Han, Y. (登録日: 2022-04-23, 公開日: 2023-05-31, 最終更新日: 2024-12-11)

主引用文献

Liu, C.,Han, Y.,Ma, Q.
Structural analysis of the siderophore-interacting protein from Vibrio anguillarum and its implications in classification of Vibrio homologs.
Biochem.Biophys.Res.Commun., 739:150979-150979, 2024

PubMed Abstract: Bacteria secrete siderophores to sequester the scarce iron in the environments, then the iron is transported into the cell in a siderophore-complexed form, which can be released by siderophore-interacting protein (SIP). Vibrio species comprise an array of serious pathogens, whose iron releasing process by SIP remains poorly understood. Herein, we report the high-resolution (1.2 Å) structure of Vibrio anguillarum SIP (VaSIP) in complex with FAD, representing the first structure of Vibrio SIP. VaSIP consists of a FAD-bound β-barrel domain and a Rossmann-fold domain connected by a linker, like other subgroup I SIPs. FAD is bound to the inter-domain cavity by aromatic stacking and hydrogen bonding interactions. Structural comparison indicated a modified NAD(P)H-binding motif (DxTA-EVL-GE) for subgroup I SIPs. The putative siderophore-binding pocket of VaSIP contains three lysines to form the basic triad to bind siderophore. Phylogenetic analysis shows Vibrio SIPs are mainly divided into two clades, represented by VaSIP and Vibrio cholerae ViuB, respectively. Interestingly, the two clades adopt distinct siderophore-binding basic triads, suggesting functional divergence among Vibrio SIPs. Our results shed light on the structural and phylogenetic characteristics of Vibrio SIPs, providing molecular basis for understanding Vibrio iron metabolism and designing anti-Vibrio drugs.

PubMed: 39549339
DOI: 10.1016/j.bbrc.2024.150979

実験手法

X-RAY DIFFRACTION (1.19 Å)