Structure of the 30S ribosomal decoding complex at ambient temperature.

Autor:	Dao EH; Stanford PULSE Institute, SLAC National Laboratory, Menlo Park, California 94025, USA., Poitevin F; Stanford PULSE Institute, SLAC National Laboratory, Menlo Park, California 94025, USA.; Department of Structural Biology, Stanford University, Palo Alto, California 94305, USA., Sierra RG; Stanford PULSE Institute, SLAC National Laboratory, Menlo Park, California 94025, USA.; Linac Coherent Light Source, SLAC National Laboratory, Menlo Park, California 94025, USA., Gati C; Department of Structural Biology, Stanford University, Palo Alto, California 94305, USA.; Biosciences Division, SLAC National Laboratory, Menlo Park, California 94025, USA., Rao Y; Stanford PULSE Institute, SLAC National Laboratory, Menlo Park, California 94025, USA.; Linac Coherent Light Source, SLAC National Laboratory, Menlo Park, California 94025, USA., Ciftci HI; Stanford PULSE Institute, SLAC National Laboratory, Menlo Park, California 94025, USA., Akşit F; Stanford PULSE Institute, SLAC National Laboratory, Menlo Park, California 94025, USA., McGurk A; Linac Coherent Light Source, SLAC National Laboratory, Menlo Park, California 94025, USA., Obrinski T; Linac Coherent Light Source, SLAC National Laboratory, Menlo Park, California 94025, USA., Mgbam P; Linac Coherent Light Source, SLAC National Laboratory, Menlo Park, California 94025, USA., Hayes B; Linac Coherent Light Source, SLAC National Laboratory, Menlo Park, California 94025, USA., De Lichtenberg C; Institutionen för Kemi, Kemiskt Biologiskt Centrum, Umeå Universitet, SE-901 87 Umeå, Sweden., Pardo-Avila F; Department of Structural Biology, Stanford University, Palo Alto, California 94305, USA., Corsepius N; Department of Structural Biology, Stanford University, Palo Alto, California 94305, USA., Zhang L; Linac Coherent Light Source, SLAC National Laboratory, Menlo Park, California 94025, USA., Seaberg MH; Linac Coherent Light Source, SLAC National Laboratory, Menlo Park, California 94025, USA., Hunter MS; Linac Coherent Light Source, SLAC National Laboratory, Menlo Park, California 94025, USA., Liang M; Linac Coherent Light Source, SLAC National Laboratory, Menlo Park, California 94025, USA., Koglin JE; Linac Coherent Light Source, SLAC National Laboratory, Menlo Park, California 94025, USA., Wakatsuki S; Department of Structural Biology, Stanford University, Palo Alto, California 94305, USA.; Biosciences Division, SLAC National Laboratory, Menlo Park, California 94025, USA., Demirci H; Stanford PULSE Institute, SLAC National Laboratory, Menlo Park, California 94025, USA.; Department of Structural Biology, Stanford University, Palo Alto, California 94305, USA.; Biosciences Division, SLAC National Laboratory, Menlo Park, California 94025, USA.
Jazyk:	angličtina
Zdroj:	RNA (New York, N.Y.) [RNA] 2018 Dec; Vol. 24 (12), pp. 1667-1676. Date of Electronic Publication: 2018 Aug 23.
DOI:	10.1261/rna.067660.118
Abstrakt:	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 Thermus thermophilus 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. (© 2018 Dao et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society.)
Databáze:	MEDLINE
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