1voz: Difference between revisions

[[Image:1voz.gif|left|200px]]

'''Crystal structure of five 70s ribosomes from Escherichia Coli in complex with protein Y. This file contains the 30s subunit of one 70s ribosome. The entire crystal structure contains five 70s ribosomes and is described in remark 400.'''

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.

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