9hrp | pdb_00009hrp

Structure of YIUA from Yersinia ruckeri with iron

spinqualitylabelsall models 9hrp, resolution 2.32Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9hrp is a 4 chain structure with sequence from Yersinia ruckeri. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.32Å Ligands: FE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A085U4N5_YERRU Publication Abstract from PubMed The marine pathogen Yersinia ruckeri synthesizes the tri-catecholate siderophore ruckerbactin, Rb, (DHB-(L)Arg-(L)Ser)(3), to acquire iron during infection. Its biosynthetic gene cluster encodes a single periplasmic binding protein, RupB, which surprisingly does not bind Fe(III)-Rb nor the Fe(III) complexes of its hydrolysis products, the di- and mono-catecholate siderophores Rb(DC) and Rb(MC), with biologically relevant affinities. Instead, the periplasmic binding protein YiuA, encoded in a different region of the chromosome, binds the 1 : 2 Fe(III) complex of the mono-catecholate Rb(MC), Fe(III)-(Rb(MC))(2). YiuA is the first periplasmic binding protein (PBP) to selectively recognize a mono-catecholate siderophore, the structural basis of which was illuminated through X-ray crystallography of YiuA bound to Fe(III)-(Rb(MC))(2). Yersinia ruckeri YRB periplasmic binding protein YiuA selectively recognizes a Fe(III)-mono-catecholate siderophore.,Thomsen E, Thompson S, Stow PR, Cukor M, Grogan G, Duhme-Klair AK, Butler A Chem Commun (Camb). 2025 Oct 16. doi: 10.1039/d5cc05103g. PMID:41098114 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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