4V4G
Crystal structure of five 70s ribosomes from Escherichia Coli in complex with protein Y.
This is a non-PDB format compatible entry.
Summary for 4V4G
| Entry DOI | 10.2210/pdb4v4g/pdb |
| Related | 1VOR 1VOS 1VOU 1VOV 1VOW 1VOX 1VOY 1VOZ 1VP0 |
| Descriptor | 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (53 entities in total) |
| Functional Keywords | 30s ribosomal subunit, protein-rna complex, protein-protein complex, rna-rna complex, ribosome |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 265 |
| Total formula weight | 10637746.99 |
| Authors | Vila-Sanjurjo, A.,Schuwirth, B.S.,Hau, C.W.,Cate, J.H. (deposition date: 2004-10-06, release date: 2014-07-09, Last modification date: 2023-12-06) |
| Primary citation | Vila-Sanjurjo, A.,Schuwirth, B.S.,Hau, C.W.,Cate, J.H. Structural basis for the control of translation initiation during stress. Nat.Struct.Mol.Biol., 11:1054-1059, 2004 Cited by PubMed 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. PubMed: 15502846DOI: 10.1038/nsmb850 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (11.5 Å) |
Structure validation
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