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PDBsum entry 2avy

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Top Page protein dna_rna metals Protein-protein interface(s) links
Ribosome PDB id
2avy
Contents
Protein chains
206 a.a.
205 a.a.
150 a.a.
100 a.a.
150 a.a.
129 a.a.
127 a.a.
98 a.a.
117 a.a.
123 a.a.
114 a.a.
96 a.a.
88 a.a.
82 a.a.
80 a.a.
55 a.a.
79 a.a.
85 a.a.
218 a.a.
51 a.a.
DNA/RNA
Metals
_MG ×60
Waters ×300

References listed in PDB file
Key reference
Title Structures of the bacterial ribosome at 3.5 a resolution.
Authors B.S.Schuwirth, M.A.Borovinskaya, C.W.Hau, W.Zhang, A.Vila-Sanjurjo, J.M.Holton, J.H.Cate.
Ref. Science, 2005, 310, 827-834. [DOI no: 10.1126/science.1117230]
PubMed id 16272117
Abstract
We describe two structures of the intact bacterial ribosome from Escherichia coli determined to a resolution of 3.5 angstroms by x-ray crystallography. These structures provide a detailed view of the interface between the small and large ribosomal subunits and the conformation of the peptidyl transferase center in the context of the intact ribosome. Differences between the two ribosomes reveal a high degree of flexibility between the head and the rest of the small subunit. Swiveling of the head of the small subunit observed in the present structures, coupled to the ratchet-like motion of the two subunits observed previously, suggests a mechanism for the final movements of messenger RNA (mRNA) and transfer RNAs (tRNAs) during translocation.
Figure 6.
Fig. 6. Molecular interactions in the intersubunit bridges. (A) Contact between S13 and L5 in ribosome I. (B) Contact between S13 and L5 in ribosome II. Only the C traces for the proteins are shown, because protein side chains are not clear in the electron density of either ribosome. Residues that become inaccessible to solvent (44) are indicated in orange for L5 and in yellow for S13 and S19. The direction of view is indicated in the center. (C) Molecular interactions in bridge B3. (D) Molecular interactions in bridge B7a. (E) Molecular interactions in bridge B6. Waters modeled at the interface are shown as red spheres inside the water-accessible volume, green mesh. (F) Close approach of phosphates at the subunit interface near bridge B2c. Distances (in angstroms) between phosphate oxygens are marked.
Figure 7.
Fig. 7. Intersubunit bridges B2a and B4. (A) Minor-groove interactions between H69 and h44 and h45, broken down by region. Atoms within hydrogen-bonding distance, as mentioned in the text, are connected by dashed lines. (B) Molecular interactions in bridge B4. Protein S15 in the 30S subunit is in blue, with relevant side chains in green. The interaction is viewed from the left side of Fig. 5A (left) and from the right side of Fig. 5A (right). Electron density is visible for the side chain of Arg88 (R88) in ribosome II, but not in ribosome I. Other amino acid abbreviations: I, Ile; L, Leu; V, Val; A, Ala; Q, Gln.
The above figures are reprinted by permission from the AAAs: Science (2005, 310, 827-834) copyright 2005.
PROCHECK
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