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Ribosome engineering to promote new crystal forms
Uppsala universitet, Teknisk-naturvetenskapliga vetenskapsområdet, Biologiska sektionen, Institutionen för cell- och molekylärbiologi, Struktur- och molekylärbiologi.
2012 (engelsk)Inngår i: Acta Crystallographica Section D: Biological Crystallography, ISSN 0907-4449, E-ISSN 1399-0047, Vol. 68, nr 5, s. 578-583Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

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.

sted, utgiver, år, opplag, sider
2012. Vol. 68, nr 5, s. 578-583
Emneord [en]
ribosome, GTPase, engineering
HSV kategori
Identifikatorer
URN: urn:nbn:se:uu:diva-174688DOI: 10.1107/S0907444912006348ISI: 000303159000009OAI: oai:DiVA.org:uu-174688DiVA, id: diva2:528789
Tilgjengelig fra: 2012-05-28 Laget: 2012-05-25 Sist oppdatert: 2017-12-07bibliografisk kontrollert

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