8RC1

MAP7 MTBD (microtubule binding domain) decorated microtubule protofilament

Summary for 8RC1

• Entry DOI: 10.2210/pdb8rc1/pdb
• EMDB information: 19042
• Descriptor: Tubulin alpha-1B chain, Tubulin beta chain, Microtubule associated protein 7 (MAP7), ... (6 entities in total)
• Functional Keywords: microtubule associated protein 7(map 7), microtubule binding domain, cryo-em, structural protein
• Biological source: Homo sapiens; More
• Total number of polymer chains: 5
• Total formula weight: 206351.03

Authors

Bangera, M.,Moores, C.A. (deposition date: 2023-12-05, release date: 2024-03-13)

Primary citation

Adler, A.,Bangera, M.,Beugelink, J.W.,Bahri, S.,van Ingen, H.,Moores, C.A.,Baldus, M.
A structural and dynamic visualization of the interaction between MAP7 and microtubules.
Nat Commun, 15:1948-1948, 2024

PubMed Abstract: Microtubules (MTs) are key components of the eukaryotic cytoskeleton and are essential for intracellular organization, organelle trafficking and mitosis. MT tasks depend on binding and interactions with MT-associated proteins (MAPs). MT-associated protein 7 (MAP7) has the unusual ability of both MT binding and activating kinesin-1-mediated cargo transport along MTs. Additionally, the protein is reported to stabilize MTs with its 112 amino-acid long MT-binding domain (MTBD). Here we investigate the structural basis of the interaction of MAP7 MTBD with the MT lattice. Using a combination of solid and solution-state nuclear magnetic resonance (NMR) spectroscopy with electron microscopy, fluorescence anisotropy and isothermal titration calorimetry, we shed light on the binding mode of MAP7 to MTs at an atomic level. Our results show that a combination of interactions between MAP7 and MT lattice extending beyond a single tubulin dimer and including tubulin C-terminal tails contribute to formation of the MAP7-MT complex.

PubMed: 38431715
DOI: 10.1038/s41467-024-46260-5

Experimental method

ELECTRON MICROSCOPY (3.7 Å)