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8FR3

E. coli EF-Tu in complex with KKL-55

Summary for 8FR3
Entry DOI10.2210/pdb8fr3/pdb
DescriptorElongation factor Tu, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
Functional Keywordsef-tu, translation, antibiotic
Biological sourceEscherichia coli K-12
Total number of polymer chains2
Total formula weight90027.93
Authors
Nguyen, H.A.,Kuzmishin Nagy, A.B.,Dunham, C.M. (deposition date: 2023-01-06, release date: 2023-09-20, Last modification date: 2023-11-29)
Primary citationMarathe, N.,Nguyen, H.A.,Alumasa, J.N.,Kuzmishin Nagy, A.B.,Vazquez, M.,Dunham, C.M.,Keiler, K.C.
Antibiotic that inhibits trans -translation blocks binding of EF-Tu to tmRNA but not to tRNA.
Mbio, 14:e0146123-e0146123, 2023
Cited by
PubMed Abstract: Elongation factor thermo-unstable (EF-Tu) is a universally conserved translation factor that mediates productive interactions between tRNAs and the ribosome. In bacteria, EF-Tu also delivers transfer-messenger RNA (tmRNA)-SmpB to the ribosome during -translation. We report the first small molecule, KKL-55, that specifically inhibits EF-Tu activity in -translation without affecting its activity in normal translation. KKL-55 has broad-spectrum antibiotic activity, suggesting that compounds targeted to the tmRNA-binding interface of EF-Tu could be developed into new antibiotics to treat drug-resistant infections.
PubMed: 37681945
DOI: 10.1128/mbio.01461-23
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.23 Å)
Structure validation

243911

数据于2025-10-29公开中

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