Structural highlights
4v4g is a 265 chain structure with sequence from Escherichia coli. This structure supersedes and combines the now removed PDB entries 1voq, 1vor, 1vos, 1vou, 1vov, 1vow, 1vox, 1voy, 1voz and 1vp0. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| NonStd Res: | |
| Related: | 1voq, 1vor, 1vos, 1vou, 1vov, 1vow, 1vox, 1voy, 1voz, 1vp0 |
| Resources: | FirstGlance, OCA, RCSB, PDBsum |
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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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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:http://dx.doi.org/10.1038/nsmb850
