PDBsum entry 3vza

Cell cycle

PDB id: 3vza

Contents

Protein chains

99 a.a.

62 a.a.

31 a.a.

Waters ×357

PDB id:

3vza

Name:

Cell cycle

Title:

Crystal structure of the chicken spc24-spc25 globular domain in complex with cenp-t peptide

Structure:

Uncharacterized protein. Chain: b, a. Fragment: rwd domain, globular domain, unp residues 132-234. Synonym: spc25 protein. Engineered: yes. Spc24 protein. Chain: d, c. Fragment: rwd domain, globular domain. Engineered: yes.

Source:

Gallus gallus. Chicken. Organism_taxid: 9031. Gene: spc25. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: cenpt. Expression_system_taxid: 562

Resolution:

1.90Å R-factor: 0.170 R-free: 0.216

Authors:

T.Nishino,T.Fukagawa

Key ref:

T.Nishino et al. (2013). CENP-T provides a structural platform for outer kinetochore assembly. Embo J, 32, 424-436. PubMed id: 23334297

Date:

09-Oct-12 Release date: 03-Apr-13

Protein chains

E1C4Y2  (E1C4Y2_CHICK) -

Protein chains

R4GRT4  (R4GRT4_CHICK) -  Kinetochore protein Spc24 from Gallus gallus

Seq: 73 a.a.

Struc: 62 a.a.

Protein chains

F1NPG5  (CENPT_CHICK) -  Centromere protein T from Gallus gallus

Seq: 639 a.a.

Struc: 31 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Embo J 32:424-436 (2013)

PubMed id: 23334297

CENP-T provides a structural platform for outer kinetochore assembly.

T.Nishino, F.Rago, T.Hori, K.Tomii, I.M.Cheeseman, T.Fukagawa.

ABSTRACT

The kinetochore forms a dynamic interface with microtubules from the mitotic spindle during mitosis. The Ndc80 complex acts as the key microtubule-binding complex at kinetochores. However, it is unclear how the Ndc80 complex associates with the inner kinetochore proteins that assemble upon centromeric chromatin. Here, based on a high-resolution structural analysis, we demonstrate that the N-terminal region of vertebrate CENP-T interacts with the 'RWD' domain in the Spc24/25 portion of the Ndc80 complex. Phosphorylation of CENP-T strengthens a cryptic hydrophobic interaction between CENP-T and Spc25 resulting in a phospho-regulated interaction that occurs without direct recognition of the phosphorylated residue. The Ndc80 complex interacts with both CENP-T and the Mis12 complex, but we find that these interactions are mutually exclusive, supporting a model in which two distinct pathways target the Ndc80 complex to kinetochores. Our results provide a model for how the multiple protein complexes at kinetochores associate in a phospho-regulated manner.