7SGS

Cryo-EM structure of full-length MAP7 bound to the microtubule

Summary for 7SGS

• Entry DOI: 10.2210/pdb7sgs/pdb
• EMDB information: 25117 25118 25119 25120
• Descriptor: Tubulin alpha-1B chain, Tubulin beta chain, Ensconsin, ... (6 entities in total)
• Functional Keywords: microtubule, microtubule-associated protein, cytoskeleton, structural protein
• Biological source: Sus scrofa (Pig); More
• Total number of polymer chains: 4
• Total formula weight: 236062.03

Authors

Ferro, L.S.,Fang, Q.,Eshun-Wilson, L.,Fernandes, J.,Jack, A.,Farrell, D.P.,Golcuk, M.,Huijben, T.,Costa, K.,Gur, M.,DiMaio, F.,Nogales, E.,Yildiz, A. (deposition date: 2021-10-07, release date: 2022-05-18, Last modification date: 2024-06-05)

Primary citation

Ferro, L.S.,Fang, Q.,Eshun-Wilson, L.,Fernandes, J.,Jack, A.,Farrell, D.P.,Golcuk, M.,Huijben, T.,Costa, K.,Gur, M.,DiMaio, F.,Nogales, E.,Yildiz, A.
Structural and functional insight into regulation of kinesin-1 by microtubule-associated protein MAP7.
Science, 375:326-331, 2022

PubMed Abstract: Microtubule (MT)-associated protein 7 (MAP7) is a required cofactor for kinesin-1-driven transport of intracellular cargoes. Using cryo-electron microscopy and single-molecule imaging, we investigated how MAP7 binds MTs and facilitates kinesin-1 motility. The MT-binding domain (MTBD) of MAP7 bound MTs as an extended α helix between the protofilament ridge and the site of lateral contact. Unexpectedly, the MTBD partially overlapped with the binding site of kinesin-1 and inhibited its motility. However, by tethering kinesin-1 to the MT, the projection domain of MAP7 prevented dissociation of the motor and facilitated its binding to available neighboring sites. The inhibitory effect of the MTBD dominated as MTs became saturated with MAP7. Our results reveal biphasic regulation of kinesin-1 by MAP7 in the context of their competitive binding to MTs.

PubMed: 35050657
DOI: 10.1126/science.abf6154

Experimental method

ELECTRON MICROSCOPY (3.3 Å)