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Mutations to kirrom...
Mutations to kirromycin resistance occur in the interface of domains I and III of EF-Tu.GTP
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- Abdulkarim, Farhad (author)
- Uppsala universitet,Institutionen för molekylärbiologi
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- Liljas, Lars (author)
- Uppsala universitet,Institutionen för molekylärbiologi
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- Hughes, Diarmaid, 1956- (author)
- Uppsala universitet,Institutionen för molekylärbiologi
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(creator_code:org_t)
- 2001-10-19
- 1994
- English.
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In: FEBS Letters. - : Wiley. - 0014-5793 .- 1873-3468. ; 352, s. 118-122
- Related links:
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https://febs.onlinel...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Subject headings
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- The antibiotic kirromycin inhibits protein synthesis by binding to EF-Tu and preventing its release from the ribosome after GTP hydrolysis.We have isolated and sequenced a collection of kirromycin resistant tuf mutations and identified thirteen single amino acid substitutions at sevendifferent sites in EF-Tu. These have been mapped onto the 3D structures of EF-Tu’GTP and EF-Tu.GDP. In the active GTP form of EF-Tu themutations cluster on each side of the interface between domains I and III. We propose that this domain interface is the binding site for kirromycin.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Mikrobiologi inom det medicinska området (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Microbiology in the medical area (hsv//eng)
Keyword
- EF-Tu
- Kirromycin
- Protein structure
- tgf mutation
- Salmonella typhimurium
- Escherichia coli
- Microbiology, immunology, infectious diseases
- Mikrobiologi, immunologi, infektionssjukdomar
Publication and Content Type
- ref (subject category)
- art (subject category)
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