4NF9

Structure of the Knl1/Nsl1 complex

Summary for 4NF9

• Entry DOI: 10.2210/pdb4nf9/pdb
• Descriptor: Protein CASC5, Kinetochore-associated protein NSL1 homolog, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: rwd domain, cell cycle
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: Q8NG31 Q96IY1
• Total number of polymer chains: 4
• Total formula weight: 58609.38

Authors

Petrovic, A.,Mosalaganti, S.,Keller, J.,Mattiuzzo, M.,Overlack, K.,Wohlgemuth, S.,Pasqualato, S.,Raunser, S.,Musacchio, A. (deposition date: 2013-10-31, release date: 2014-03-19)

Primary citation

Petrovic, A.,Mosalaganti, S.,Keller, J.,Mattiuzzo, M.,Overlack, K.,Krenn, V.,De Antoni, A.,Wohlgemuth, S.,Cecatiello, V.,Pasqualato, S.,Raunser, S.,Musacchio, A.
Modular Assembly of RWD Domains on the Mis12 Complex Underlies Outer Kinetochore Organization.
Mol.Cell, 53:591-605, 2014

PubMed Abstract: Faithful chromosome segregation is mandatory for cell and organismal viability. Kinetochores, large protein assemblies embedded in centromeric chromatin, establish a mechanical link between chromosomes and spindle microtubules. The KMN network, a conserved 10-subunit kinetochore complex, harbors the microtubule-binding interface. RWD domains in the KMN subunits Spc24 and Spc25 mediate kinetochore targeting of the microtubule-binding subunits by interacting with the Mis12 complex, a KMN subcomplex that tethers directly onto the underlying chromatin layer. Here, we show that Knl1, a KMN subunit involved in mitotic checkpoint signaling, also contains RWD domains that bind the Mis12 complex and that mediate kinetochore targeting of Knl1. By reporting the first 3D electron microscopy structure of the KMN network, we provide a comprehensive framework to interpret how interactions of RWD-containing proteins with the Mis12 complex shape KMN network topology. Our observations unveil a regular pattern in the construction of the outer kinetochore.

PubMed: 24530301
DOI: 10.1016/j.molcel.2014.01.019

Experimental method

X-RAY DIFFRACTION (2.8 Å)