1vor | pdb_00001vor

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.

spinqualitylabelsall models 1vor, resolution 11.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1vor is a 32 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: MSE Related: 1voq, 1vos, 1vou, 1vov, 1vow, 1vox, 1voy, 1voz, 1vp0 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. 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. See Also Ribosome 3D structures

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