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Publication Abstract from PubMed

Iron-sulfur (Fe-S) clusters are ubiquitous and are necessary to sustain basic life processes. The intracellular Fe-S clusters do not form spontaneously and many proteins are required for their biosynthesis and delivery. The bacterial P-loop NTPase family protein ApbC participates in Fe-S cluster assembly and transfers the cluster into apoproteins, with the Walker A motif and CxxC motif being essential for functionality of ApbC in Fe-S protein biogenesis. However, the structural basis underlying the ApbC activity and the motifs' role remains unclear. Here, we report the crystal structure of Escherichia coli ApbC at 2.8 A resolution. The dimeric structure is in a W shape and the active site is located in the 2-fold center. The function of the motifs can be annotated by structural analyses. ApbC has an additional N-terminal domain that differs from other P-loop NTPases, possibly conferring its inherent specificity in vivo.

Crystal structure of the iron-sulfur cluster transfer protein ApbC from Escherichia coli.,Yang J, Duan YF, Liu L Biochem Biophys Res Commun. 2024 May 23;722:150167. doi: , 10.1016/j.bbrc.2024.150167. PMID:38797154^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.