7SQK

Cryo-EM structure of the human augmin complex

Summary for 7SQK

• Entry DOI: 10.2210/pdb7sqk/pdb
• EMDB information: 25387
• Descriptor: HAUS augmin-like complex subunit 1, HAUS augmin-like complex subunit 2, HAUS augmin-like complex subunit 3, ... (8 entities in total)
• Functional Keywords: cell division, mitosis, microtubules, cell cycle
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 8
• Total formula weight: 379182.81

Authors

Gabel, C.A.,Chang, L. (deposition date: 2021-11-05, release date: 2022-09-21, Last modification date: 2024-06-05)

Primary citation

Gabel, C.A.,Li, Z.,DeMarco, A.G.,Zhang, Z.,Yang, J.,Hall, M.C.,Barford, D.,Chang, L.
Molecular architecture of the augmin complex.
Nat Commun, 13:5449-5449, 2022

PubMed Abstract: Accurate segregation of chromosomes during mitosis depends on the correct assembly of the mitotic spindle, a bipolar structure composed mainly of microtubules. The augmin complex, or homologous to augmin subunits (HAUS) complex, is an eight-subunit protein complex required for building robust mitotic spindles in metazoa. Augmin increases microtubule density within the spindle by recruiting the γ-tubulin ring complex (γ-TuRC) to pre-existing microtubules and nucleating branching microtubules. Here, we elucidate the molecular architecture of augmin by single particle cryo-electron microscopy (cryo-EM), computational methods, and crosslinking mass spectrometry (CLMS). Augmin's highly flexible structure contains a V-shaped head and a filamentous tail, with the head existing in either extended or contracted conformational states. Our work highlights how cryo-EM, complemented by computational advances and CLMS, can elucidate the structure of a challenging protein complex and provides insights into the function of augmin in mediating microtubule branching nucleation.

PubMed: 36114186
DOI: 10.1038/s41467-022-33227-7

Experimental method

ELECTRON MICROSCOPY (8 Å)