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The 2.3 MDa 70S ribosome presents a formidable target for solution-state NMR, yet resonances can be detected from more flexible regions of the complex, such as the L7/L12 stalk region. This has allowed detailed studies of the structure and dynamics of the stalk region, which due to its flexibility is not readily observable by X-ray crystallography or cryo-electron microscopy.

The ribosome is the target for about half of all known antibiotics, which work by preventing bacterial ribosomes from making new proteins. Ultimately, an enhanced understanding of structure and dynamics during biosynthesis could result in novel antibiotic design strategies.

Further reading:

• Archaeal MBF1 binds to 30S and 70S ribosomes via its helix-turn-helix domain. Blombach F, Launay HM, Snijders APL, Zorraquino V, Wu H, de Koning  B, Brouns SJJ, Ettema TJG, Camilloni C, Cavalli A, Vendruscolo M, Dickman MJ, Cabrita LD, La Teana A, Benelli D, Londei P, Christodoulou J, van der Oost J. Biochem J (2014) 462, 373-384. pubmed | pdf
• Heteronuclear NMR investigations of dynamic regions of intact E. coli ribosomes. Christodoulou J, Larsson G, Fucini P, Connell S, Pertinhez TA, Hanson CL, Redfield C, Nierhaus KH, Robinson CV, Schleucher J, Dobson CM. PNAS (2004) 101, 10949-10954. pubmed | pdf