1XVY
Crystal Structure of iron-free Serratia marcescens SfuA
Summary for 1XVY
Entry DOI | 10.2210/pdb1xvy/pdb |
Related | 1XVX |
Descriptor | sfuA, CITRIC ACID (3 entities in total) |
Functional Keywords | periplasmic iron binding protein, iron binding protein |
Biological source | Yersinia enterocolitica |
Cellular location | Periplasm (Probable): P21408 |
Total number of polymer chains | 1 |
Total formula weight | 33509.79 |
Authors | Shouldice, S.R.,McRee, D.E.,Dougan, D.R.,Tari, L.W.,Schryvers, A.B. (deposition date: 2004-10-28, release date: 2004-12-14, Last modification date: 2023-08-23) |
Primary citation | Shouldice, S.R.,McRee, D.E.,Dougan, D.R.,Tari, L.W.,Schryvers, A.B. Novel Anion-independent Iron Coordination by Members of a Third Class of Bacterial Periplasmic Ferric Ion-binding Proteins J.Biol.Chem., 280:5820-5827, 2005 Cited by PubMed Abstract: 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. PubMed: 15576371DOI: 10.1074/jbc.M411238200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.74 Å) |
Structure validation
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