Fig. 6
From: Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s
KLP10A neck-linker docking. The figure shows the structure of the beginning of the neck-linker domain present in the KLP10A protein constructs (six residues at the C-terminal end of the motor domain). a NMMTapo. b NMMTAMP-PNP. c CTMMTAMP-PNP Neck-linker in red, KLP10A motor domain in blue, β-tubulin in orange, α-tubulin in yellow, corresponding cryo-EM map density as a gray mesh. d CTMMTAMP-PNP. structure with neck-linker in the up docked position. Core motor domain solvent exclusion surface colored by hydrophobicity with neck-linker shown as ribbon and atom sticks (Kyte and Doolittle hydrophobicity scale with orange to blue representing more to less hydrophobicity). Residue L610 colored red and shown as a ball and stick atom representation. e Close up of the image d showing the KLP10A residues forming the hydrophobic pocket where residue L610 plugs into. Residue K608 marks the end of α-helix 6 and the beginning of the neck linker. f Aligned neck linker sequences of six kinesins-13s (DmKLP10A, DmKLP59C, DmKLP59D, HsKIF2A, HsKIF2B, and HSKIF2C) and seven motile kinesins (DmKHC, HsKIF5B, HsKIF5A, DmKLP61F, HsKIF11, DmKLP64D, and DmNCD). Dm Drosophila melanogaster, Hs Homo sapiens. Asterisk is aligned with DmKLP10A K608. Arrow is aligned with DmKLP10A L610. Structures oriented in a–e with the tubulin plus-end at the top. H4 α-helix 4, NL Neck-linker, βS1 β-strand 1
