4WSF: Falafel EVH1 domain bound to CENP-C FIM

Citation:
Abstract
The cell division cycle requires tight coupling between protein phosphorylation and dephosphorylation. However, understanding the cell cycle roles of multimeric protein phosphatases has been limited by the lack of knowledge of how their diverse regulatory subunits target highly conserved catalytic subunits to their sites of action. Phosphoprotein phosphatase 4 (PP4) has been recently shown to participate in the regulation of cell cycle progression. We now find that the EVH1 domain of the regulatory subunit 3 of Drosophila PP4, Falafel (Flfl), directly interacts with the centromeric protein C (CENP-C). Unlike other EVH1 domains that interact with proline-rich ligands, the crystal structure of the Flfl amino-terminal EVH1 domain bound to a CENP-C peptide reveals a new target-recognition mode for the phosphatase subunit. We also show that binding of Flfl to CENP-C is required to bring PP4 activity to centromeres to maintain CENP-C and attached core kinetochore proteins at chromosomes during mitosis.
PDB ID: 4WSFDownload
MMDB ID: 125526
PDB Deposition Date: 2014/10/27
Updated in MMDB: 2014/12
Experimental Method:
x-ray diffraction
Resolution: 1.501  Å
Source Organism:
Drosophila melanogaster
Similar Structures:
Biological Unit for 4WSF: dimeric; determined by author and by software (PISA)
Molecular Components in 4WSF
Label Count Molecule
Proteins (2 molecules)
1
Serine/threonine-protein Phosphatase 4 Regulatory Subunit 3(Gene symbol: flfl)
Molecule annotation
1
Cenp-c
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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