7me1
YfeA oligomer crystal 1, form 1
Structural highlights
FunctionYFEA_YERPE Part of an ATP-driven transport system YfeABCD for chelated iron. Publication Abstract from PubMedThe substrate-binding protein YfeA (also known as YPO2439 or y1897) is a polyspecific metal-binding protein that is crucial for nutrient acquisition and virulence in Yersinia pestis, the causative microbe of plague. YfeA folds into a monomeric c-clamp like other substrate-binding proteins and has two metal-binding sites (sites 1 and 2). Site 2 is a bidentate surface site capable of binding Zn and Mn atoms and is a unique feature of YfeA. Occasionally, the site 2 residues of two YfeA molecules will cooperate with the histidine tag of a third YfeA molecule in coordinating the same metal and lead to metal-dependent crystallographic packing. Here, three crystal structures of YfeA are presented at 1.85, 2.05 and 2.25 A resolution. A comparison of the structures reveals that the metal can be displaced at five different locations ranging from approximately 4 to approximately 16 A away from the canonical site 2. These observations reveal different configurations of site 2 that enable cooperative metal binding and demonstrate how site 2 is dynamic and freely available for inter-protein metal coordination. Site 2 of the Yersinia pestis substrate-binding protein YfeA is a dynamic surface metal-binding site.,Radka CD, Aller SG Acta Crystallogr F Struct Biol Commun. 2021 Sep 1;77(Pt 9):286-293. doi:, 10.1107/S2053230X21008086. Epub 2021 Aug 24. PMID:34473105[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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