期刊
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
卷 68, 期 -, 页码 578-583出版社
WILEY-BLACKWELL
DOI: 10.1107/S0907444912006348
关键词
ribosome; GTPase; engineering
资金
- Wenner-Gren foundations
- Swedish Research council
- Swedish foundation for Strategic Research
- UK Medical Research Council
- Wellcome Trust
- Agouron Institute
- Louis-Jeantet Foundation
- Medical Research Council [MC_U105184332] Funding Source: researchfish
- MRC [MC_U105184332] Funding Source: UKRI
Crystallographic studies of the ribosome have provided molecular details of protein synthesis. However, the crystallization of functional complexes of ribosomes with GTPase translation factors proved to be elusive for a decade after the first ribosome structures were determined. Analysis of the packing in different 70S ribosome crystal forms revealed that regardless of the species or space group, a contact between ribosomal protein L9 from the large subunit and 16S rRNA in similar to the shoulder of a neighbouring small subunit in the crystal lattice competes with the binding of GTPase elongation factors to this region of 16S rRNA. To prevent the formation of this preferred crystal contact, a mutant strain of Thermus thermophilus, HB8-MRCMSAW1, in which the ribosomal protein L9 gene has been truncated was constructed by homologous recombination. Mutant 70S ribosomes were used to crystallize and solve the structure of the ribosome with EF-G, GDP and fusidic acid in a previously unobserved crystal form. Subsequent work has shown the usefulness of this strain for crystallization of the ribosome with other GTPase factors.
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