1ob5
From Proteopedia
(New page: 200px<br /> <applet load="1ob5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ob5, resolution 3.10Å" /> '''T. AQUATICUS ELONGA...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1OB5 is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]] with MG, C, PHA, GNP and ENX as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.48 3.6.1.48]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OB5 OCA]]. | + | 1OB5 is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]] with MG, C, PHA, GNP and ENX as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Transferred_entry:_3.6.5.3 Transferred entry: 3.6.5.3]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.48 3.6.1.48]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OB5 OCA]]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Thermus aquaticus]] | [[Category: Thermus aquaticus]] | ||
| + | [[Category: Transferred entry: 3.6.5.3]] | ||
[[Category: Dahlberg, C.]] | [[Category: Dahlberg, C.]] | ||
[[Category: Nielsen, R.C.]] | [[Category: Nielsen, R.C.]] | ||
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[[Category: translation elongation factor]] | [[Category: translation elongation factor]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:12:03 2007'' |
Revision as of 09:07, 30 October 2007
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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 ... [(full description)]
About this Structure
1OB5 is a [Protein complex] structure of sequences from [Thermus aquaticus] with MG, C, PHA, GNP and ENX as [ligands]. Active as [Transferred entry: 3.6.5.3], with EC number [3.6.1.48]. Structure known Active Site: AC1. 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 Tue Oct 30 11:12:03 2007
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
