4ZGO

Structure of C-terminally truncated Cdc123 from Schizosaccharomyces pombe

Summary for 4ZGO

• Entry DOI: 10.2210/pdb4zgo/pdb
• Descriptor: Cell division cycle protein 123 (2 entities in total)
• Functional Keywords: atp-grap fold, cell cycle, eif2 assembly
• Biological source: Schizosaccharomyces pombe (Fission yeast)
• Cellular location: Cytoplasm : Q9P7N5
• Total number of polymer chains: 2
• Total formula weight: 78220.49

Authors

Panvert, M.,Dubiez, E.,Arnold, L.,Perez, J.,Seufert, W.,Mechulam, Y.,Schmitt, E. (deposition date: 2015-04-23, release date: 2015-09-30, Last modification date: 2024-05-01)

Primary citation

Panvert, M.,Dubiez, E.,Arnold, L.,Perez, J.,Mechulam, Y.,Seufert, W.,Schmitt, E.
Cdc123, a Cell Cycle Regulator Needed for eIF2 Assembly, Is an ATP-Grasp Protein with Unique Features.
Structure, 23:1596-1608, 2015

PubMed 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.

PubMed: 26211610
DOI: 10.1016/j.str.2015.06.014

Experimental method

X-RAY DIFFRACTION (2.063 Å)