6CAO

Structure of the ribosomal decoding complex at ambient temperature

Summary for 6CAO

• Entry DOI: 10.2210/pdb6cao/pdb
• Descriptor: 16S Ribosomal RNA rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (28 entities in total)
• Functional Keywords: ribosome, translation, decoding
• Biological source: Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579); More
• Total number of polymer chains: 23
• Total formula weight: 786460.88

Authors

DeMirci, H. (deposition date: 2018-01-31, release date: 2018-07-25, Last modification date: 2019-04-17)

Primary citation

Dao, E.H.,Poitevin, F.,Sierra, R.G.,Gati, C.,Rao, Y.,Ciftci, H.I.,Aksit, F.,McGurk, A.,Obrinski, T.,Mgbam, P.,Hayes, B.,De Lichtenberg, C.,Pardo-Avila, F.,Corsepius, N.,Zhang, L.,Seaberg, M.H.,Hunter, M.S.,Liang, M.,Koglin, J.E.,Wakatsuki, S.,Demirci, H.
Structure of the 30S ribosomal decoding complex at ambient temperature.
RNA, 24:1667-1676, 2018

PubMed Abstract: The ribosome translates nucleotide sequences of messenger RNA to proteins through selection of cognate transfer RNA according to the genetic code. To date, structural studies of ribosomal decoding complexes yielding high-resolution data have predominantly relied on experiments performed at cryogenic temperatures. New light sources like the X-ray free electron laser (XFEL) have enabled data collection from macromolecular crystals at ambient temperature. Here, we report an X-ray crystal structure of the 30S ribosomal subunit decoding complex to 3.45 Å resolution using data obtained at ambient temperature at the Linac Coherent Light Source (LCLS). We find that this ambient-temperature structure is largely consistent with existing cryogenic-temperature crystal structures, with key residues of the decoding complex exhibiting similar conformations, including adenosine residues 1492 and 1493. Minor variations were observed, namely an alternate conformation of cytosine 1397 near the mRNA channel and the A-site. Our serial crystallography experiment illustrates the amenability of ribosomal microcrystals to routine structural studies at ambient temperature, thus overcoming a long-standing experimental limitation to structural studies of RNA and RNA-protein complexes at near-physiological temperatures.

PubMed: 30139800
DOI: 10.1261/rna.067660.118

Experimental method

X-RAY DIFFRACTION (3.45 Å)