4ZGN

Structure Cdc123 complexed with the C-terminal domain of eIF2gamma

4ZGN の概要

• エントリーDOI: 10.2210/pdb4zgn/pdb
• 分子名称: Cell division cycle protein 123, Eukaryotic translation initiation factor 2 subunit gamma, ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: atp-grasp fold, cell cycle, eif2 assembly
• 由来する生物種: Schizosaccharomyces pombe (Fission yeast); 詳細
• 細胞内の位置: Cytoplasm : Q9P7N5
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 52618.92

構造登録者

Panvert, M.,Dubiez, E.,Arnold, L.,Perez, J.,Seufert, W.,Mechulam, Y.,Schmitt, E. (登録日: 2015-04-23, 公開日: 2015-09-30, 最終更新日: 2024-10-23)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.9 Å)