7XLZ

Structure of siderophore-interacting protein from Vibrio anguillarum

Summary for 7XLZ

• Entry DOI: 10.2210/pdb7xlz/pdb
• Descriptor: Siderophore-interacting protein, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: siderophore-interacting protein, iron release, vibrio anguillarum, oxidoreductase
• Biological source: Vibrio anguillarum (strain ATCC 68554 / 775) (Listonella anguillarum)
• Total number of polymer chains: 2
• Total formula weight: 61674.52

Authors

Ma, Q.,Liu, C.,Han, Y. (deposition date: 2022-04-23, release date: 2023-05-31, Last modification date: 2024-12-11)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.19 Å)