8ZKC

iron-sulfur cluster transfer protein ApbC

Summary for 8ZKC

• Entry DOI: 10.2210/pdb8zkc/pdb
• Descriptor: Iron-sulfur cluster carrier protein, GLYCEROL, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: iron-sulfur clusters, dimerization, disulfide bonds, cytosolic protein
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 44323.25

Authors

Yang, J.,Liu, L. (deposition date: 2024-05-16, release date: 2024-06-12)

Primary citation

Yang, J.,Duan, Y.F.,Liu, L.
Crystal structure of the iron-sulfur cluster transfer protein ApbC from Escherichia coli.
Biochem.Biophys.Res.Commun., 722:150167-150167, 2024

PubMed Abstract: 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 Å 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.

PubMed: 38797154
DOI: 10.1016/j.bbrc.2024.150167

Experimental method

X-RAY DIFFRACTION (2.85 Å)