1ob5

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[[Image:1ob5.gif|left|200px]]<br /><applet load="1ob5" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ob5.gif|left|200px]]
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caption="1ob5, resolution 3.10&Aring;" />
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'''T. AQUATICUS ELONGATION FACTOR EF-TU COMPLEXED WITH THE ANTIBIOTIC ENACYLOXIN IIA, A GTP ANALOG, AND PHE-TRNA'''<br />
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{{Structure
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|PDB= 1ob5 |SIZE=350|CAPTION= <scene name='initialview01'>1ob5</scene>, resolution 3.10&Aring;
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|SITE= <scene name='pdbsite=AC1:Enx+Binding+Site+For+Chain+E'>AC1</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=C:CYTIDINE-5'-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=PHA:PHENYLALANINAL'>PHA</scene>, <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene> and <scene name='pdbligand=ENX:ENACYLOXIN IIA'>ENX</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''T. AQUATICUS ELONGATION FACTOR EF-TU COMPLEXED WITH THE ANTIBIOTIC ENACYLOXIN IIA, A GTP ANALOG, AND PHE-TRNA'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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 <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=C:'>C</scene>, <scene name='pdbligand=PHA:'>PHA</scene>, <scene name='pdbligand=GNP:'>GNP</scene> and <scene name='pdbligand=ENX:'>ENX</scene> 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] Known structural/functional Site: <scene name='pdbsite=AC1:Enx+Binding+Site+For+Chain+E'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OB5 OCA].
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1OB5 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OB5 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16257965 16257965]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16257965 16257965]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Thermus aquaticus]]
[[Category: Thermus aquaticus]]
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[[Category: translation elongation factor]]
[[Category: translation elongation factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:15:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:08:21 2008''

Revision as of 11:08, 20 March 2008

Image:1ob5.gif


PDB ID 1ob5

Drag the structure with the mouse to rotate
, resolution 3.10Å
Sites:
Ligands: , , , and
Activity: Transferred entry: 3.6.5.3, with EC number 3.6.1.48
Coordinates: save as pdb, mmCIF, xml



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. 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

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