PDBsum entry 4zgo

Cell cycle

PDB id: 4zgo

Contents

Protein chains

252 a.a.

Waters ×198

PDB id:

4zgo

Name:

Cell cycle

Title:

Structure of c-terminally truncated cdc123 from schizosaccharomyces pombe

Structure:

Cell division cycle protein 123. Chain: a, b. Fragment: unp residues 21-389. Engineered: yes

Source:

Schizosaccharomyces pombe. Fission yeast. Organism_taxid: 4896. Gene: cdc123, spap27g11.03. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.06Å R-factor: 0.195 R-free: 0.230

Authors:

M.Panvert,E.Dubiez,L.Arnold,J.Perez,W.Seufert,Y.Mechulam,E.Schmitt

Key ref:

M.Panvert et al. (2015). Cdc123, a Cell Cycle Regulator Needed for eIF2 Assembly, Is an ATP-Grasp Protein with Unique Features. Structure, 23, 1596-1608. PubMed id: 26211610 DOI: 10.1016/j.str.2015.06.014

Date:

23-Apr-15 Release date: 30-Sep-15

Protein chains

Q9P7N5  (CD123_SCHPO) -  Translation initiation factor eIF2 assembly protein from Schizosaccharomyces pombe (strain 972 / ATCC 24843)

Seq: 319 a.a.

Struc: 252 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.str.2015.06.014

Structure 23:1596-1608 (2015)

PubMed id: 26211610

Cdc123, a Cell Cycle Regulator Needed for eIF2 Assembly, Is an ATP-Grasp Protein with Unique Features.

M.Panvert, E.Dubiez, L.Arnold, J.Perez, Y.Mechulam, W.Seufert, E.Schmitt.

ABSTRACT

Eukaryotic initiation factor 2 (eIF2), a heterotrimeric guanosine triphosphatase, has a central role in protein biosynthesis by supplying methionylated initiator tRNA to the ribosomal translation initiation complex and by serving as a target for translational control in response to stress. Recent work identified a novel step indispensable for eIF2 function: assembly of eIF2 from its three subunits by the cell proliferation protein Cdc123. We report the first crystal structure of a Cdc123 representative, that from Schizosaccharomyces pombe, both isolated and bound to domain III of Saccharomyces cerevisiae eIF2γ. The structures show that Cdc123 resembles enzymes of the ATP-grasp family. Indeed, Cdc123 binds ATP-Mg(2+), and conserved residues contacting ATP-Mg(2+) are essential for Cdc123 to support eIF2 assembly and cell viability. A docking of eIF2αγ onto Cdc123, combined with genetic and biochemical experiments, allows us to propose a model explaining how Cdc123 participates in the biogenesis of eIF2 through facilitating assembly of eIF2γ to eIF2α.