Publication Abstract from PubMed
Crystal structures of FbpA, the periplasmic ferric ion-binding protein of an iron-uptake ABC transporter, from Thermus thermophilus HB8 (TtFbpA) have been solved in apo and ferric ion-bound forms at 1.8 and 1.7 A resolution, respectively. The latter crystal structure shows that the bound ferric ion forms a novel six-coordinated complex with three tyrosine side chains, two bicarbonates and a water molecule in the metal-binding site. The results of gel-filtration chromatography and dynamic light scattering show that TtFbpA exists as a monomer in solution regardless of ferric ion binding and that TtFbpA adopts a more compact conformation in the ferric ion-bound state than in the apo state in solution.
A novel mode of ferric ion coordination by the periplasmic ferric ion-binding subunit FbpA of an ABC-type iron transporter from Thermus thermophilus HB8.,Wang S, Ogata M, Horita S, Ohtsuka J, Nagata K, Tanokura M Acta Crystallogr D Biol Crystallogr. 2014 Jan;70(Pt 1):196-202. doi:, 10.1107/S1399004713026333. Epub 2013 Dec 31. PMID:24419392[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
