Search: onr:"swepub:oai:lup.lub.lu.se:d04204ce-470c-464e-8022-5d048f843474" >
The dynamic structu...
The dynamic structure of EF-G studied by fusidic acid resistance and internal revertants
-
- Johanson, U (author)
- Uppsala University,Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
-
Aevarsson, A (author)
-
- Liljas, A (author)
- Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
-
show more...
-
- Hughes, D (author)
- Uppsala University
-
show less...
-
(creator_code:org_t)
- Elsevier BV, 1996
- 1996
- English 13 s.
-
In: Journal of Molecular Biology. - : Elsevier BV. - 0022-2836. ; 258:3, s. 32-420
- Related links:
-
http://dx.doi.org/10... (free)
-
show more...
-
https://lup.lub.lu.s...
-
https://doi.org/10.1...
-
show less...
Abstract
Subject headings
Close
- We have previously identified 20 different fusidic acid-resistant alleles of fusA, encoding mutant forms of the ribosomal translocase EF-G. One of these, P413L, is used here as the starting point in selections for internal revertants, identifying 20 different pseudo-wild-type forms of EF-G. We have also identified two alleles of fusA previously isolated as suppressors of 4.5 S RNA deficiency. All of these mutants are analysed in terms of their effects on the structural dynamics of EF-G. Most mutation conferring fusidic acid-resistance interfere with conformational changes of EF-G, but some may be located at a possible fusidic acid binding site. Revertants of the P413L mutations restore the function of EF-G with or without affecting the level of resistance to fusidic acid. The revertant mutations probably restore the balance between the GDP and GTP conformations of EF-G off the ribosome, and most of them are located close to the interface between the G domain and domain II. The procedure for the isolation of pseudo-wild-type forms of EF-G can be used to direct evolution progressively away from the wild-type while still maintaining the essential functions of EF-G.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
- NATURVETENSKAP -- Biologi -- Mikrobiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Microbiology (hsv//eng)
Keyword
- Anti-Bacterial Agents
- Binding Sites
- DNA Mutational Analysis
- Directed Molecular Evolution
- Drug Resistance, Microbial
- Escherichia coli
- Fusidic Acid
- Models, Molecular
- Mutation
- Peptide Elongation Factor G
- Peptide Elongation Factors
- Protein Structure, Tertiary
- Protein Synthesis Inhibitors
- RNA, Ribosomal
- Salmonella typhimurium
- Spectinomycin
- Suppression, Genetic
- Thermus thermophilus
- Journal Article
- Research Support, Non-U.S. Gov't
Publication and Content Type
- art (subject category)
- ref (subject category)
Find in a library
To the university's database