3v22 | pdb_00003v22

Crystal structure of RMF bound to the 70S ribosome. This PDB entry contains coordinates for the 30S subunit with bound RMF of the 1st ribosome in the ASU

spinqualitylabelsall models 3v22, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3v22 is a 22 chain structure with sequence from Escherichia coli and Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG, ZN Related: 3v23, 3v24, 3v25 Gene: rmf (Escherichia coli) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Eubacteria inactivate their ribosomes as 100S dimers or 70S monomers upon entry into stationary phase. In Escherichia coli, 100S dimer formation is mediated by ribosome modulation factor (RMF) and hibernation promoting factor (HPF), or alternatively, the YfiA protein inactivates ribosomes as 70S monomers. Here, we present high-resolution crystal structures of the Thermus thermophilus 70S ribosome in complex with each of these stationary-phase factors. The binding site of RMF overlaps with that of the messenger RNA (mRNA) Shine-Dalgarno sequence, which prevents the interaction between the mRNA and the 16S ribosomal RNA. The nearly identical binding sites of HPF and YfiA overlap with those of the mRNA, transfer RNA, and initiation factors, which prevents translation initiation. The binding of RMF and HPF, but not YfiA, to the ribosome induces a conformational change of the 30S head domain that promotes 100S dimer formation. How hibernation factors RMF, HPF, and YfiA turn off protein synthesis.,Polikanov YS, Blaha GM, Steitz TA Science. 2012 May 18;336(6083):915-8. PMID:22605777 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosomal protein THX Ribosome 3D structures

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