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Crystals 2017, 7(2), 37; doi:10.3390/cryst7020037

Crystal Structure of the 23S rRNA Fragment Specific to r-Protein L1 and Designed Model of the Ribosomal L1 Stalk from Haloarcula marismortui

Institute of Protein Research, Russian Academy of Sciences, Institutskaya 4, 142290 Puschino, Moscow Region, Russian Federation
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Received: 13 December 2016 / Accepted: 29 January 2017 / Published: 2 February 2017
(This article belongs to the Special Issue Recent Advances in Protein Crystallography)
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Abstract

The crystal structure of the 92-nucleotide L1-specific fragment of 23S rRNA from Haloarcula marismortui (Hma) has been determined at 3.3 Å resolution. Similar to the corresponding bacterial rRNA fragments, this structure contains joined helix 76-77 topped by an approximately globular structure formed by the residual part of the L1 stalk rRNA. The position of HmaL1 relative to the rRNA was found by its docking to the rRNA fragment using the L1-rRNA complex from Thermus thermophilus as a guide model. In spite of the anomalous negative charge of the halophilic archaeal protein, the conformation of the HmaL1-rRNA interface appeared to be very close to that observed in all known L1-rRNA complexes. The designed structure of the L1 stalk was incorporated into the H. marismortui 50S ribosomal subunit. Comparison of relative positions of L1 stalks in 50S subunits from H. marismortui and T. thermophilus made it possible to reveal the site of inflection of rRNA during the ribosome function. View Full-Text
Keywords: Haloarcula marismortui; ribosomes; archaea; 23S rRNA; X-ray crystallography Haloarcula marismortui; ribosomes; archaea; 23S rRNA; X-ray crystallography
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Gabdulkhakov, A.; Tishchenko, S.; Mikhaylina, A.; Garber, M.; Nevskaya, N.; Nikonov, S. Crystal Structure of the 23S rRNA Fragment Specific to r-Protein L1 and Designed Model of the Ribosomal L1 Stalk from Haloarcula marismortui. Crystals 2017, 7, 37.

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