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. 2022 Sep 6;11:e77877. doi: 10.7554/eLife.77877

Figure 6. Microtubule binding interface of kinesin-4 KLP-12 at β-tubulin helix H12.

(A) Close-up display of KLP-12 and β-tubulin interaction around β-tubulin helix H12 from the same view as upper panel (middle panel) and 45° rotated view (bottom panel). Glu410 of β-tubulin H12 interacts with Arg311 and Arg317 of KLP-12 helix α5. Tyr150 and Asn151 of KLP-12 form intramolecular interactions. See Video 3 for detail. The interfaces of KIF5B and KIF2C at β-tubulin are available in Figure 5—figure supplement 1. (B) Sequence alignment with the secondary structure of the kinesin-4, KIF5B, and KIF2C residues at the interacting area. (C) Superimposition of Cα chain trace models of the KLP-12 complex (orange) and KIF5B complex (green) at kinesin around β-tubulin H12. (D) Superimposition of Cα chain trace models of the KLP-12 complex (orange) and KIF2C complex (cyan) at kinesin around β-tubulin H12.

Figure 6.

Figure 6—figure supplement 1. Microtubule binding interface of KIF5B and KIF2C at β-tubulin helix H12.

Figure 6—figure supplement 1.

(A) KIF5B and β-tubulin interface. Glu420 (bovine Glu420 corresponds to Glu410 of porcine) of β-tubulin H12 has no interaction with KIF5B; instead, KIF5B Glu157 forms an intramolecular interaction with Arg278 and Arg284 of KIF5B α5. (B) KIF2C and β-tubulin interaction. Glu420 (bovine Glu420 corresponds to Glu410 of porcine) of β-tubulin H12 interacts with Arg540 of KIF2C α5. Tyr405 and Asn406 of KIF2C form intramolecular interactions. In addition, KIF2C Arg420, which is supported by Leu422, interacts with Asp414 and Glu417 of β-tubulin H12.