Fig. 3: MAS NMR spectra and conformations of functionally important regions of KIF5B bound to MTs. | Nature Communications

Fig. 3: MAS NMR spectra and conformations of functionally important regions of KIF5B bound to MTs.

From: Magic-angle-spinning NMR structure of the kinesin-1 motor domain assembled with microtubules reveals the elusive neck linker orientation

Fig. 3

a Left: binding site of KIF5B (purple) in complex with MTs (cyan); Right: An expanded view of the KIF5B-tubulin dimer interface showing the interacting helices and loops. b Nucleotide-binding region in the apo-KIF5B structure. The T87 in P-loop is distant from E236, indicating the “open” state of nucleotide-binding pocket. Carbon, nitrogen, oxygen and sulfur atoms are colored with purple, cyan, orange and red, respectively. Hydrogen atoms are not shown. c Expansions of 2D CORD spectra of [1,6-13C-glucose,U-15N]-KIF5B/MT (cyan), [2-13C-glucose,U-15N]-KIF5B/MT (purple) and U-13C,15N-KIF5B/MT (gray) illustrating long-range correlations with the neck linker. Distance restraint network between neck linker and nearby residues within KIF5B mapped onto the structure is shown in black dashed lines. d Expansion of the superposition of 2D CORD spectra of apo-KIF5B/MT (gray) and ADP-KIF5B/MT (purple) illustrating chemical shift and peak intensity changes. Assigned peaks with pronounced changes are labeled in the spectra. e–g Regions that comprise residues for which chemical shift and/or intensity changes are observed in the CORD spectra, mapped onto MAS NMR structure of KIF5B bound to MTs. Undocked neck linker in apo-KIF5B e; Expected region for docked neck linker in ADP-KIF5B f; and nucleotide binding cleft g.

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