1ob5
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Elongation factor (EF-) Tu.GTP is the carrier of aminoacyl-tRNA to the | + | Elongation factor (EF-) Tu.GTP is the carrier of aminoacyl-tRNA to the programmed ribosome. Enacyloxin IIa inhibits bacterial protein synthesis by hindering the release of EF-Tu.GDP from the ribosome. The crystal structure of the Escherichia coli EF-Tu.guanylyl iminodiphosphate (GDPNP).enacyloxin IIa complex at 2.3 A resolution presented here reveals the location of the antibiotic at the interface of domains 1 and 3. The binding site overlaps that of kirromycin, an antibiotic with a structure that is unrelated to enacyloxin IIa but that also inhibits EF-Tu.GDP release. As one of the major differences, the enacyloxin IIa tail borders a hydrophobic pocket that is occupied by the longer tail of kirromycin, explaining the higher binding affinity of the latter. EF-Tu.GDPNP.enacyloxin IIa shows a disordered effector region that in the Phe-tRNAPhe.EF-Tu (Thermus aquaticus).GDPNP.enacyloxin IIa complex, solved at 3.1 A resolution, is stabilized by the interaction with tRNA. This work clarifies the structural background of the action of enacyloxin IIa and compares its properties with those of kirromycin, opening new perspectives for structure-guided design of novel antibiotics. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Thermus aquaticus]] | [[Category: Thermus aquaticus]] | ||
| - | [[Category: Transferred entry: 3 | + | [[Category: Transferred entry: 3 6.5 3]] |
[[Category: Dahlberg, C.]] | [[Category: Dahlberg, C.]] | ||
| - | [[Category: Nielsen, R | + | [[Category: Nielsen, R C.]] |
[[Category: Nissen, P.]] | [[Category: Nissen, P.]] | ||
[[Category: Nyborg, J.]] | [[Category: Nyborg, J.]] | ||
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[[Category: translation elongation factor]] | [[Category: translation elongation factor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:15:36 2008'' |
Revision as of 12:15, 21 February 2008
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T. AQUATICUS ELONGATION FACTOR EF-TU COMPLEXED WITH THE ANTIBIOTIC ENACYLOXIN IIA, A GTP ANALOG, AND PHE-TRNA
Overview
Elongation factor (EF-) Tu.GTP is the carrier of aminoacyl-tRNA to the programmed ribosome. Enacyloxin IIa inhibits bacterial protein synthesis by hindering the release of EF-Tu.GDP from the ribosome. The crystal structure of the Escherichia coli EF-Tu.guanylyl iminodiphosphate (GDPNP).enacyloxin IIa complex at 2.3 A resolution presented here reveals the location of the antibiotic at the interface of domains 1 and 3. The binding site overlaps that of kirromycin, an antibiotic with a structure that is unrelated to enacyloxin IIa but that also inhibits EF-Tu.GDP release. As one of the major differences, the enacyloxin IIa tail borders a hydrophobic pocket that is occupied by the longer tail of kirromycin, explaining the higher binding affinity of the latter. EF-Tu.GDPNP.enacyloxin IIa shows a disordered effector region that in the Phe-tRNAPhe.EF-Tu (Thermus aquaticus).GDPNP.enacyloxin IIa complex, solved at 3.1 A resolution, is stabilized by the interaction with tRNA. This work clarifies the structural background of the action of enacyloxin IIa and compares its properties with those of kirromycin, opening new perspectives for structure-guided design of novel antibiotics.
About this Structure
1OB5 is a Protein complex structure of sequences from Thermus aquaticus with , , , and as ligands. Active as Transferred entry: 3.6.5.3, with EC number 3.6.1.48 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Enacyloxin IIa pinpoints a binding pocket of elongation factor Tu for development of novel antibiotics., Parmeggiani A, Krab IM, Watanabe T, Nielsen RC, Dahlberg C, Nyborg J, Nissen P, J Biol Chem. 2006 Feb 3;281(5):2893-900. Epub 2005 Oct 28. PMID:16257965
Page seeded by OCA on Thu Feb 21 14:15:36 2008
Categories: Protein complex | Thermus aquaticus | Transferred entry: 3 6.5 3 | Dahlberg, C. | Nielsen, R C. | Nissen, P. | Nyborg, J. | Parmeggiani, A. | C | ENX | GNP | MG | PHA | Gtp-binding | Gtpase | Hydrolase | Nucleotide-binding | Protein biosynthesis | Transfer rna | Translation elongation factor
