SNAP annotations: PDB entry 4v4g

PDB-id

4v4g; DSSR-derived features in text and JSON formats; DNAproDB

Class

ribosome

Method

X-ray (11.5 Å)

Summary

Crystal structure of five 70s ribosomes from escherichia coli in complex with protein y.

Reference

Vila-Sanjurjo A, Schuwirth BS, Hau CW, Cate JH (2004): "Structural basis for the control of translation initiation during stress." Nat.Struct.Mol.Biol., 11, 1054-1059. doi: 10.1038/nsmb850.

Abstract

During environmental stress, organisms limit protein synthesis by storing inactive ribosomes that are rapidly reactivated when conditions improve. Here we present structural and biochemical data showing that protein Y, an Escherichia coli stress protein, fills the tRNA- and mRNA-binding channel of the small ribosomal subunit to stabilize intact ribosomes. Protein Y inhibits translation initiation during cold shock but not at normal temperatures. Furthermore, protein Y competes with conserved translation initiation factors that, in bacteria, are required for ribosomal subunit dissociation. The mechanism used by protein Y to reduce translation initiation during stress and quickly release ribosomes for renewed translation initiation may therefore occur widely in nature.