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1voy

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1voy, resolution 11.50Å ()
Non-Standard Residues:
Related: 1voq, 1vor, 1vos, 1vou, 1vov, 1vow, 1vox, 1voz, 1vp0
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


Contents

Crystal structure of five 70s ribosomes from Escherichia Coli in complex with protein Y. This file contains the 50s subunit of one 70s ribosome. The entire crystal structure contains five 70s ribosomes and is described in remark 400.

Publication Abstract from PubMed

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.

Structural basis for the control of translation initiation during stress., Vila-Sanjurjo A, Schuwirth BS, Hau CW, Cate JH, Nat Struct Mol Biol. 2004 Nov;11(11):1054-9. Epub 2004 Oct 24. PMID:15502846

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1voy is a 32 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

See Also

Reference

  • Vila-Sanjurjo A, Schuwirth BS, Hau CW, Cate JH. Structural basis for the control of translation initiation during stress. Nat Struct Mol Biol. 2004 Nov;11(11):1054-9. Epub 2004 Oct 24. PMID:15502846 doi:10.1038/nsmb850

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