6q1c | pdb_00006q1c
Apo YfeA extracted from the E. coli periplasm
Structural highlights
FunctionYFEA_YERPE Part of an ATP-driven transport system YfeABCD for chelated iron. Publication Abstract from PubMedIn the structural biology of bacterial substrate-binding proteins (SBPs), a growing number of comparisons between substrate-bound and substrate-free forms of metal atom-binding (cluster A-I) SBPs have revealed minimal structural differences between forms. These observations contrast with SBPs that bind substrates such as amino acids or nucleic acids and may undergo >60 degrees rigid-body rotations. Substrate transfer in these SBPs is described by a Venus flytrap model, although this model may not apply to all SBPs. In this report, structures are presented of substrate-free (apo) and reconstituted substrate-bound (holo) YfeA, a polyspecific cluster A-I SBP from Yersinia pestis. It is demonstrated that an apo cluster A-I SBP can be purified by fractionation when co-expressed with its cognate transporter, adding an alternative strategy to the mutagenesis or biochemical treatment used to generate other apo cluster A-I SBPs. The apo YfeA structure contains 111 disordered protein atoms in a mobile helix located in the flexible carboxy-terminal lobe. Metal binding triggers a 15-fold reduction in the solvent-accessible surface area of the metal-binding site and reordering of the 111 protein atoms in the mobile helix. The flexible lobe undergoes a 13.6 degrees rigid-body rotation that is driven by a spring-hammer metal-binding mechanism. This asymmetric rigid-body rotation may be unique to metal atom-binding SBPs (i.e. clusters A-I, A-II and D-IV). Structures of the substrate-binding protein YfeA in apo and zinc-reconstituted holo forms.,Radka CD, Labiuk SL, DeLucas LJ, Aller SG Acta Crystallogr D Struct Biol. 2019 Sep 1;75(Pt 9):831-840. doi: , 10.1107/S2059798319010866. Epub 2019 Aug 22. PMID:31478906[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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