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2c78

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[[Image:2c78.gif|left|200px]]
[[Image:2c78.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2c78 |SIZE=350|CAPTION= <scene name='initialview01'>2c78</scene>, resolution 1.4&Aring;
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The line below this paragraph, containing "STRUCTURE_2c78", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Pul+Binding+Site+For+Chain+A'>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=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PUL:(1S,2S,3E,5E,7E,10S,11S,12S)-12-[(2R,4E,6E,8Z,10R,12E,14E,16Z,18S,19Z)-10,18-DIHYDROXY-12,16,19-TRIMETHYL-11,22-DIOXOOXACYCLODOCOSA-4,6,8,12,14,16,19-HEPTAEN-2-YL]-2,11-DIHYDROXY-1,10-DIMETHYL-9-OXOTRIDECA-3,5,7-TRIEN-1-YL+6-DEOXY-2,4-DI-O-METHYL-BETA-L-GALACTOPYRANOSIDE'>PUL</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/dGTPase dGTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.5.1 3.1.5.1] </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_2c78| PDB=2c78 | 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=2c78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c78 OCA], [http://www.ebi.ac.uk/pdbsum/2c78 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c78 RCSB]</span>
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}}
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'''EF-TU COMPLEXED WITH A GTP ANALOG AND THE ANTIBIOTIC PULVOMYCIN'''
'''EF-TU COMPLEXED WITH A GTP ANALOG AND THE ANTIBIOTIC PULVOMYCIN'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: dGTPase]]
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[[Category: DGTPase]]
[[Category: Krab, I M.]]
[[Category: Krab, I M.]]
[[Category: Nielsen, R C.]]
[[Category: Nielsen, R C.]]
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[[Category: Okamura, S.]]
[[Category: Okamura, S.]]
[[Category: Parmeggiani, A.]]
[[Category: Parmeggiani, A.]]
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[[Category: antibiotic]]
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[[Category: Antibiotic]]
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[[Category: elongation factor]]
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[[Category: Elongation factor]]
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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: phosphorylation]]
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[[Category: Phosphorylation]]
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[[Category: protein biosynthesis]]
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[[Category: Protein biosynthesis]]
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[[Category: protein synthesis]]
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[[Category: Protein synthesis]]
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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 21:22:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:17:21 2008''
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Revision as of 18:22, 3 May 2008

Image:2c78.gif

Template:STRUCTURE 2c78

EF-TU COMPLEXED WITH A GTP ANALOG AND THE ANTIBIOTIC PULVOMYCIN


Overview

Pulvomycin inhibits protein synthesis by preventing the formation of the ternary complex between elongation factor Tu (EF-Tu) x GTP and aa-tRNA. In this work, the crystal structure of Thermus thermophilus EF-Tu x pulvomycin in complex with the GTP analogue guanylyl imino diphosphate (GDPNP) at 1.4 A resolution reveals an antibiotic binding site extending from the domain 1-3 interface to domain 2, overlapping the domain 1-2-3 junction. Pulvomycin binding interferes with the binding of the 3'-aminoacyl group, the acceptor stem, and 5' end of tRNA. Only part of pulvomycin overlaps the binding site of GE2270 A, a domain 2-bound antibiotic of a structure unrelated to pulvomycin, which also hinders aa-tRNA binding. The structure of the T. thermophilus EF-Tu x GDPNP x GE2270 A complex at 1.6 A resolution shows that GE2270 A interferes with the binding of the 3'-aminoacyl group and part of the acceptor stem of aa-tRNA but not with the 5' end. Both compounds, pulvomycin more markedly, hinder the correct positioning of domain 1 over domains 2 and 3 that characterizes the active form of EF-Tu, while they affect the domain 1 switch regions that control the EF-Tu x GDP/GTP transitions in different ways. This work reveals how two antibiotics with different structures and binding modes can employ a similar mechanism of action.

About this Structure

2C78 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Structural basis of the action of pulvomycin and GE2270 A on elongation factor Tu., Parmeggiani A, Krab IM, Okamura S, Nielsen RC, Nyborg J, Nissen P, Biochemistry. 2006 Jun 6;45(22):6846-57. PMID:16734421 Page seeded by OCA on Sat May 3 21:22:11 2008

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