1xvx
From Proteopedia
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Crystal Structure of iron-loaded Yersinia enterocolitica YfuA
Overview
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.
About this Structure
1XVX is a Single protein structure of sequence from Yersinia enterocolitica with FE, ZN, CO3 and EDO as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Nov 25 03:02:59 2007
