Next Article in Journal
Hydrothermal Crystal Growth of Piezoelectric α-Quartz Phase of AO2 (A = Ge, Si) and MXO4 (M = Al, Ga, Fe and X = P, As): A Historical Overview
Next Article in Special Issue
The Synergetic Effects of Combining Structural Biology and EPR Spectroscopy on Membrane Proteins
Previous Article in Journal
Simple Metal and Binary Alloy Phases Based on the fcc Structure: Electronic Origin of Distortions, Superlattices and Vacancies
Previous Article in Special Issue
Crystal Structure of the Substrate-Binding Domain from Listeria monocytogenes Bile-Resistance Determinant BilE
Article Menu
Issue 2 (February) cover image

Export Article

Open AccessArticle
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
Author to whom correspondence should be addressed.
Received: 13 December 2016 / Accepted: 29 January 2017 / Published: 2 February 2017
(This article belongs to the Special Issue Recent Advances in Protein Crystallography)
View Full-Text   |   Download PDF [13316 KB, uploaded 14 February 2017]   |  


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

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

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.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Crystals EISSN 2073-4352 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top