Protein Translocation Channels in the Proteasome and Other Proteases

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Proteasome & other proteases Proteasome - core complex and regulatory cap Other proteases - HslUV, ClpAP, ClpXP, Lon, FtsH 19-1.

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Protein Translocation Channels in the Proteasome and Other Proteases Christopher N Larsen, Daniel Finley Cell Volume 91, Issue 4, Pages 431-434 (November 1997) DOI: 10.1016/S0092-8674(00)80427-4

Figure 1 Proteasomes from Eukaryotes and Archaea Magenta, regulatory complex. Blue, core particle. Green, slice surface. Red dots, active sites. Cyan dots, N termini. Note that in (C) and in Figure 2F, cyan indicates the most N-terminal residue visualized, Thr-13 and Ser-11, respectively. (D)–(E) compiled with assistance of L. Ditzel and R. Huber. (A) Electron micrograph of proteasome holoenzyme from a representative eukaryote (X. laevis). (B) Medial cut-away view of the T. acidophilum proteasome core particle (Baumeister and Lupas 1997). The lumen is divided into three chambers, and the central chamber contains the peptidase active sites (red). (C) Ribbon diagram of two T. acidophilum α subunits, showing the structure of the pore channel. (D) Cut-away view of the S. cerevisiae proteasome core particle. (E) Ribbon diagram of two S. cerevisiae α subunits (Left: Pre10/Prs1; Right: Pre9/Y13). The N termini of these subunits are shown to occlude the channel. Cell 1997 91, 431-434DOI: (10.1016/S0092-8674(00)80427-4)

Figure 2 HslVU and ClpAP Proteases Color scheme as in Figure 1. Compiled with assistance from L. Ditzel, R. Huber, H. Kwon, and T. Ellenberger. (A) Electron micrograph of HslVU. The identity of the uppermost, asymmetrically distributed mass is unknown. (B) Cut-away view of HslV. (C) Ribbon diagram of two HslV subunits. Note proximity of the active-site Thr-1 to the pore. The C terminus has been truncated to reduce the image size. (D) Electron micrograph of ClpAP (Kessel et al. 1995). Each cap particle has a distal and proximal ring of mass density. These may correspond to the two ATPase domains of ClpA. (E) Cut-away view of ClpP. (F) Ribbon diagram of two ClpP subunits. Cell 1997 91, 431-434DOI: (10.1016/S0092-8674(00)80427-4)

Figure 3 Cut-Away Views of ATP-Independent, Proteasome-Like Complexes Compiled with assistance from T. Tamura, W. Baumeister, and N. Straeter. (A) The tricorn protease. Note that in (A) and (B) the two-fold symmetry of the image results from the placement of the section plane, which is not a symmetry plane. (B) S. cerevisiae Gal6. (C) Bovine leucine aminopeptidase. Cell 1997 91, 431-434DOI: (10.1016/S0092-8674(00)80427-4)