5KMG

Near-atomic cryo-EM structure of PRC1 bound to the microtubule

Summary for 5KMG

• Entry DOI: 10.2210/pdb5kmg/pdb
• Related: 2NRY 3NRX
• EMDB information: 8266
• Descriptor: Tubulin alpha-1B chain, Tubulin beta chain, Protein regulator of cytokinesis 1, ... (7 entities in total)
• Functional Keywords: cytoskeleton, mitosis, microtubule, microtubule-associated protein, structural protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 3
• Total formula weight: 114628.02

Authors

Kellogg, E.H.,Howes, S.,Ti, S.-C.,Ramirez-Aportela, E.,Kapoor, T.M.,Chacon, P.,Nogales, E. (deposition date: 2016-06-27, release date: 2016-08-03, Last modification date: 2024-03-06)

Primary citation

Kellogg, E.H.,Howes, S.,Ti, S.C.,Ramirez-Aportela, E.,Kapoor, T.M.,Chacon, P.,Nogales, E.
Near-atomic cryo-EM structure of PRC1 bound to the microtubule.
Proc.Natl.Acad.Sci.USA, 113:9430-9439, 2016

PubMed Abstract: Proteins that associate with microtubules (MTs) are crucial to generate MT arrays and establish different cellular architectures. One example is PRC1 (protein regulator of cytokinesis 1), which cross-links antiparallel MTs and is essential for the completion of mitosis and cytokinesis. Here we describe a 4-Å-resolution cryo-EM structure of monomeric PRC1 bound to MTs. Residues in the spectrin domain of PRC1 contacting the MT are highly conserved and interact with the same pocket recognized by kinesin. We additionally found that PRC1 promotes MT assembly even in the presence of the MT stabilizer taxol. Interestingly, the angle of the spectrin domain on the MT surface corresponds to the previously observed cross-bridge angle between MTs cross-linked by full-length, dimeric PRC1. This finding, together with molecular dynamic simulations describing the intrinsic flexibility of PRC1, suggests that the MT-spectrin domain interface determines the geometry of the MT arrays cross-linked by PRC1.

PubMed: 27493215
DOI: 10.1073/pnas.1609903113

Experimental method

ELECTRON MICROSCOPY (3.5 Å)