4P0T

Crystal structure of human centromere protein M

Summary for 4P0T

• Entry DOI: 10.2210/pdb4p0t/pdb
• Descriptor: Centromere protein M, GLYCEROL (3 entities in total)
• Functional Keywords: mitosis, kinetochore, ccan, g-protein, cell cycle
• Biological source: Homo sapiens (Human)
• Cellular location: Nucleus: Q9NSP4
• Total number of polymer chains: 2
• Total formula weight: 38582.98

Authors

Basilico, F.,Pasqualato, S.,Musacchio, A. (deposition date: 2014-02-22, release date: 2014-07-09, Last modification date: 2024-05-08)

Primary citation

Basilico, F.,Maffini, S.,Weir, J.R.,Prumbaum, D.,Rojas, A.M.,Zimniak, T.,De Antoni, A.,Jeganathan, S.,Voss, B.,van Gerwen, S.,Krenn, V.,Massimiliano, L.,Valencia, A.,Vetter, I.R.,Herzog, F.,Raunser, S.,Pasqualato, S.,Musacchio, A.
The pseudo GTPase CENP-M drives human kinetochore assembly.
Elife, 3:e02978-e02978, 2014

PubMed Abstract: Kinetochores, multi-subunit complexes that assemble at the interface with centromeres, bind spindle microtubules to ensure faithful delivery of chromosomes during cell division. The configuration and function of the kinetochore-centromere interface is poorly understood. We report that a protein at this interface, CENP-M, is structurally and evolutionarily related to small GTPases but is incapable of GTP-binding and conformational switching. We show that CENP-M is crucially required for the assembly and stability of a tetramer also comprising CENP-I, CENP-H, and CENP-K, the HIKM complex, which we extensively characterize through a combination of structural, biochemical, and cell biological approaches. A point mutant affecting the CENP-M/CENP-I interaction hampers kinetochore assembly and chromosome alignment and prevents kinetochore recruitment of the CENP-T/W complex, questioning a role of CENP-T/W as founder of an independent axis of kinetochore assembly. Our studies identify a single pathway having CENP-C as founder, and CENP-H/I/K/M and CENP-T/W as CENP-C-dependent followers.DOI: http://dx.doi.org/10.7554/eLife.02978.001.

PubMed: 25006165
DOI: 10.7554/eLife.02978

Experimental method

X-RAY DIFFRACTION (1.493 Å)