PDBsum entry 4zgn

Cell cycle

PDB id: 4zgn

Contents

Protein chains

279 a.a.

103 a.a.

Ligands

ATP

Metals

_MG

Waters ×5

PDB id:

4zgn

Name:

Cell cycle

Title:

Structure cdc123 complexed with thE C-terminal domain of eif2gamma

Structure:

Cell division cycle protein 123. Chain: a. Engineered: yes. Eukaryotic translation initiation factor 2 subunit gamma. Chain: b. Fragment: residues 410-527. Synonym: eif-2-gamma. Engineered: yes

Source:

Schizosaccharomyces pombe. Fission yeast. Organism_taxid: 284812. Gene: cdc123, spap27g11.03. Expressed in: escherichia coli. Expression_system_taxid: 562. Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 559292.

Resolution:

2.90Å R-factor: 0.198 R-free: 0.262

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 chain

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

Seq: 319 a.a.

Struc: 279 a.a.

Protein chain

P32481  (IF2G_YEAST) -  Eukaryotic translation initiation factor 2 subunit gamma from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 527 a.a.

Struc: 103 a.a.

Enzyme reactions

• Enzyme class: Chain B: E.C.3.6.5.3 - protein-synthesizing GTPase.
• Reaction: GTP + H2O = GDP + phosphate + H⁺

GTP (Bound ligand (Het Group name = ATP) matches with 96.88% similarity) + H2O = GDP + phosphate + H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

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.