Fig. 1: Cryo-EM characterization of the K20-CC-Tail/K11-CC-Tail/KAP-1 complex. | Nature Communications

Fig. 1: Cryo-EM characterization of the K20-CC-Tail/K11-CC-Tail/KAP-1 complex.

From: A mutual co-recognition mechanism ensures the proper assembly of heterotrimeric kinesin-2 for intraflagellar transport

Fig. 1

a Domain organization of KLP-20, KLP-11 and KAP-1. Both KLP-20 and KLP-11 contain an N-terminal motor domain, a neck coil (NC), the coiled-coil stalks (CC1–CC3) followed by a C-terminal tail domain. HTS, hetero-pairing trigger sequence. KAP-1 contains 11 armadillo (ARM) repeats and a N-terminal domain (NTD) with unknown functions. The residues numbers for each domain are indicated above the domain organization. Protein constructs used for cryo-EM characterization are marked by lines under the domain organization. b Representative 2D-classification averages of cryo-EM datasets. The white arrow-heads indicate the orientation of the coiled-coil stalks. c Cryo-EM reconstruction of the K20-CC-Tail/K11-CC-Tail/KAP-1 heterotrimeric complex, showing distinctive ARM-repeat structural features. d Segmentation of the cryo-EM reconstruction of the K20-CC-Tail/K11-CC-Tail/KAP-1 complex. The EM density corresponding to KAP-1 is shown in dark cyan with the extra EM densities shown in pink. The AlphaFold2-predicted KAP-1 structural model is fitted into the cryo-EM density map. e Schematic model of the KLP-20/KLP-11/KAP-1 complex showing the intrinsic flexibilities of the N-terminal region of KAP-1 and the flexible CC2-CC3 orientation of the KLP-20/KLP-11 motor heterodimer.

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