Fig. 1: Cryo-EM reconstruction of human mitochondrial ClpXPX-linked.
From: Cryo-EM structures of human ClpXP reveal mechanisms of assembly and proteolytic activation
a Cryo-EM map of the hClpXPX-linked complex with a substrate peptide bound. Each subunit of the hClpX homo-hexamer is colored distinctly. b Atomic structural model of hClpXP. The substrate peptide within the hClpX central pore is modeled as poly-alanine. The hClpX subunits are labeled A-F with the nucleotide states indicated. Chain F, the seam subunit, is disengaged from the substrate. c Top view of the hClpP map with the hClpX LGF loops (shown as helices) occupying the hydrophobic pocket. An empty LGF loop binding pocket is located between chains D and E. d Cut-away view of the hClpXPX-linked 3D reconstruction highlighting several features: pore-1 loops, nucleotides, LGF loops, the hClpP N-terminal β-hairpins, and the active site. The inset shows Y327 from the pore-1 loops forming a spiral staircase around the substrate peptide backbone.
