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From Proteopedia
Crystal Structure of iron-free Serratia marcescens SfuA
Structural highlights
FunctionFBPA_SERMA Part of the ABC transporter complex FbpABC (TC 3.A.1.10.1) involved in Fe(3+) ions import. This protein specifically binds Fe(3+) and is involved in its transmembrane transport (By similarity). 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 PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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