Fig. 3
From: Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s
Reshaping of the KLP10A–tubulin interface. a–c Side views highlighting selected areas of the KLP10A motor domain and tubulin interface undergoing conformational changes. Inset at the right of each panel shows a zoomed view the nucleotide pocket. Central β-sheet strands in dark blue; Switch-1 loop in green, Switch-2 and H4 in magenta, L2, L7, L8 and H6 in light blue. The three areas of tubulin–KLP10A interaction (I–III) are indicated. Note the line connecting the three interacting areas highlighting their different relative positions in the NMMTapo and NMMTAMP-PNP (a, b) relative to the CTMMTAMP-PNP complex (c). d P-loop aligned central β-sheets of the three complexes, NMMTapo and NMMTAMP-PNP in light semi-transparent blue and CTMMTAMP-PNP in dark blue. Numbers indicate the strand order in the KLP10A sequence. e, f Superimposed KLP10A model structures aligned on the top β-tubulin subunit (β-1). e NMMTapo. f CTMMTAMP-PNP. Closing of the KLP10A nucleotide pocket is associated with a ~12° rotation of between monomers of the bound tubulin (24° per tubulin heterodimer)
