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. 2017 Aug 3;6:1318. [Version 1] doi: 10.12688/f1000research.11683.1

Figure 1. Structure of the Cdc48/p97 ATPase.

Figure 1.

( A) Cdc48 is a homohexamer, and each monomer comprises an N-terminal (N) domain (red) and two AAA ATPase domains: D1 (blue) and D2 (green). The N-terminal (D1) side of the central pore is referred to as the cis side, and the C-terminal (D2) side as the trans side. ( B) ATP binding produces an upward rotation of the N domains into a so-called “up conformation”, in which they are positioned above the plane of the D1 ring. Left, ADP-bound state (PDB code 5FTK); right, ATPγS-bound state (PDB code 5FTN). PDB, Protein Data Bank.