1ob5

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[[Image:1ob5.gif|left|200px]]
[[Image:1ob5.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1ob5 |SIZE=350|CAPTION= <scene name='initialview01'>1ob5</scene>, resolution 3.10&Aring;
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The line below this paragraph, containing "STRUCTURE_1ob5", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Enx+Binding+Site+For+Chain+E'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=2MG:2N-METHYLGUANOSINE-5&#39;-MONOPHOSPHATE'>2MG</scene>, <scene name='pdbligand=5MC:5-METHYLCYTIDINE-5&#39;-MONOPHOSPHATE'>5MC</scene>, <scene name='pdbligand=5MU:5-METHYLURIDINE+5&#39;-MONOPHOSPHATE'>5MU</scene>, <scene name='pdbligand=7MG:7N-METHYL-8-HYDROGUANOSINE-5&#39;-MONOPHOSPHATE'>7MG</scene>, <scene name='pdbligand=A:ADENOSINE-5&#39;-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5&#39;-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=ENX:ENACYLOXIN+IIA'>ENX</scene>, <scene name='pdbligand=G:GUANOSINE-5&#39;-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=H2U:5,6-DIHYDROURIDINE-5&#39;-MONOPHOSPHATE'>H2U</scene>, <scene name='pdbligand=M2G:N2-DIMETHYLGUANOSINE-5&#39;-MONOPHOSPHATE'>M2G</scene>, <scene name='pdbligand=MAD:6-HYDRO-1-METHYLADENOSINE-5&#39;-MONOPHOSPHATE'>MAD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OMC:O2&#39;-METHYLYCYTIDINE-5&#39;-MONOPHOSPHATE'>OMC</scene>, <scene name='pdbligand=OMG:O2&#39;-METHYLGUANOSINE-5&#39;-MONOPHOSPHATE'>OMG</scene>, <scene name='pdbligand=PHA:PHENYLALANINAL'>PHA</scene>, <scene name='pdbligand=PSU:PSEUDOURIDINE-5&#39;-MONOPHOSPHATE'>PSU</scene>, <scene name='pdbligand=U:URIDINE-5&#39;-MONOPHOSPHATE'>U</scene>, <scene name='pdbligand=YG:WYBUTOSINE'>YG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-synthesizing_GTPase Protein-synthesizing GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.3 3.6.5.3] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1ob5| PDB=1ob5 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ob5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ob5 OCA], [http://www.ebi.ac.uk/pdbsum/1ob5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ob5 RCSB]</span>
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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'''
'''T. AQUATICUS ELONGATION FACTOR EF-TU COMPLEXED WITH THE ANTIBIOTIC ENACYLOXIN IIA, A GTP ANALOG, AND PHE-TRNA'''
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[[Category: Nyborg, J.]]
[[Category: Nyborg, J.]]
[[Category: Parmeggiani, A.]]
[[Category: Parmeggiani, A.]]
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[[Category: gtp-binding]]
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[[Category: Gtp-binding]]
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[[Category: gtpase]]
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[[Category: Gtpase]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: nucleotide-binding]]
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[[Category: Nucleotide-binding]]
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[[Category: protein biosynthesis]]
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[[Category: Protein biosynthesis]]
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[[Category: transfer rna]]
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[[Category: Transfer rna]]
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[[Category: translation elongation factor]]
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[[Category: Translation elongation factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:37:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:42:37 2008''
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Revision as of 00:37, 3 May 2008

Template:STRUCTURE 1ob5

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 Page seeded by OCA on Sat May 3 03:37:16 2008

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