1xvx | pdb_00001xvx

Crystal Structure of iron-loaded Yersinia enterocolitica YfuA

spinqualitylabelsall models 1xvx, resolution 1.53Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1xvx is a 1 chain structure with sequence from "bacterium_enterocoliticum"_schleifstein_and_coleman_1939 "bacterium enterocoliticum" schleifstein and coleman 1939. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CO3, EDO, FE, ZN Gene: yfuA ("Bacterium enterocoliticum" Schleifstein and Coleman 1939) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The uptake of the element iron is vital for the survival of most organisms. Numerous pathogenic Gram-negative bacteria utilize a periplasm-to-cytosol ATP-binding cassette transport pathway to transport this essential atom in to the cell. In this study, we investigated the Yersinia enterocolitica (YfuA) and Serratia marcescens (SfuA) iron-binding periplasmic proteins. We have determined the 1.8-angstroms structures of iron-loaded (YfuA) and iron-free (SfuA) forms of this class of proteins. Although the sequence of these proteins varies considerably from the other members of the transferrin structural superfamily, they adopt the same three-dimensional fold. The iron-loaded YfuA structure illustrates the unique nature of this new class of proteins in that they are able to octahedrally coordinate the ferric ion in the absence of a bound anion. The iron-free SfuA structure contains a bound citrate anion in the iron-binding cleft that tethers the N- and C-terminal domains of the apo protein and stabilizes the partially open structure. Novel anion-independent iron coordination by members of a third class of bacterial periplasmic ferric ion-binding proteins.,Shouldice SR, McRee DE, Dougan DR, Tari LW, Schryvers AB J Biol Chem. 2005 Feb 18;280(7):5820-7. Epub 2004 Dec 2. PMID:15576371 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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