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. 2015 Dec 3;6:8781. doi: 10.1038/ncomms9781

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The MsVpsΔMIT pseudohexamer is represented as a cartoon, with identical protomers shown in the same colour. (left panel) The nucleotide-free pseudohexamer; (middle panel) the pseudohexamer may bind six ATP (yellow sphere), which are probably required to assemble the catalytic active ring structure; (right panel) ATP hydrolysis generates intermediate states, which leads at one point of the cycle to an intermediate conformation that binds one ADP with high affinity and five with low affinity. The position of the arginine fingers, the glutamate (174 and 176) V interface residues, the pore loop glutamate (214) and phenylalanine 126 are indicated. These residues are required for ATPase activity and most probably participate in the transfer of ATP hydrolysis-induced conformational changes of two opposing monomers to their neighbours, thereby powering the disassembly of ESCRT-III substrate complexes via the central pore47,52.