2c77

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[[Image:2c77.gif|left|200px]]<br /><applet load="2c77" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2c77.gif|left|200px]]
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caption="2c77, resolution 1.60&Aring;" />
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'''EF-TU COMPLEXED WITH A GTP ANALOG AND THE ANTIBIOTIC GE2270 A'''<br />
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{{Structure
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|PDB= 2c77 |SIZE=350|CAPTION= <scene name='initialview01'>2c77</scene>, resolution 1.60&Aring;
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|SITE= <scene name='pdbsite=AC1:Peg+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=GEA:GE2270A'>GEA</scene> and <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''EF-TU COMPLEXED WITH A GTP ANALOG AND THE ANTIBIOTIC GE2270 A'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2C77 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=GNP:'>GNP</scene>, <scene name='pdbligand=GEA:'>GEA</scene> and <scene name='pdbligand=PEG:'>PEG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=AC1:Peg+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C77 OCA].
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2C77 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C77 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16734421 16734421]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16734421 16734421]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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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 16:45:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:11:44 2008''

Revision as of 14:11, 20 March 2008

Image:2c77.gif


PDB ID 2c77

Drag the structure with the mouse to rotate
, resolution 1.60Å
Sites:
Ligands: , , and
Activity: dGTPase, with EC number 3.1.5.1
Coordinates: save as pdb, mmCIF, xml



EF-TU COMPLEXED WITH A GTP ANALOG AND THE ANTIBIOTIC GE2270 A


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

2C77 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

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