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2c77

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Revision as of 08:23, 10 September 2015

EF-Tu complexed with a GTP analog and the antibiotic GE2270 A

Structural highlights

2c77 is a 2 chain structure with sequence from Planobispora rosea and Thet8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
NonStd Res:	, , , , , ,
Related:	1d8t, 1e9w, 1oln, 2jq7, 2zjp, 3cf5, 2c78
Activity:	dGTPase, with EC number 3.1.5.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[EFTU2_THET8] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. [THCL_PLARO] Has bacteriocidal activity against Gram-positive bacteria and a few Gram-negative bacteria. It is particularly active against anaerobes. Inhibits bacterial protein biosynthesis by preventing the formation of a stable complex between the elongation factor Tu (EF-Tu), GTP and tRNA, hindering the activation of EF-Tu.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Parmeggiani A, Krab IM, Okamura S, Nielsen RC, Nyborg J, Nissen P. Structural basis of the action of pulvomycin and GE2270 A on elongation factor Tu. Biochemistry. 2006 Jun 6;45(22):6846-57. PMID:16734421 doi:10.1021/bi0525122

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2c77"

@@ Line 2: / Line 2: @@
 <StructureSection load='2c77' size='340' side='right' caption='[[2c77]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2c77]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Planobispora_rosea Planobispora rosea] and [http://en.wikipedia.org/wiki/Thermus_thermophilus_hb8 Thermus thermophilus hb8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C77 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C77 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2c77]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Planobispora_rosea Planobispora rosea] and [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C77 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C77 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BB6:(2Z)-2-AMINO-3-SULFANYLBUT-2-ENOIC+ACID'>BB6</scene>, <scene name='pdbligand=BB7:(2Z)-2-AMINO-4-METHOXY-3-SULFANYLBUT-2-ENOIC+ACID'>BB7</scene>, <scene name='pdbligand=BB8:(2S,3S)-BETA-HYDROXY-PHENYLALANINE'>BB8</scene>, <scene name='pdbligand=BB9:(2Z)-2-AMINO-3-SULFANYLPROP-2-ENOIC+ACID'>BB9</scene>, <scene name='pdbligand=MEN:N-METHYL+ASPARAGINE'>MEN</scene>, <scene name='pdbligand=MH6:3-HYDROXY-2-IMINOPROPANOIC+ACID'>MH6</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d8t|1d8t]], [[1e9w|1e9w]], [[1oln|1oln]], [[2jq7|2jq7]], [[2zjp|2zjp]], [[3cf5|3cf5]], [[2c78|2c78]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c77 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c77 RCSB], [http://www.ebi.ac.uk/pdbsum/2c77 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c77 OCA], [http://pdbe.org/2c77 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c77 RCSB], [http://www.ebi.ac.uk/pdbsum/2c77 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2c77" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 37: / Line 38: @@
 </StructureSection>
 [[Category: Planobispora rosea]]
-[[Category: Thermus thermophilus hb8]]
+[[Category: Thet8]]
 [[Category: DGTPase]]
 [[Category: Krab, I M]]

2c77

From Proteopedia

Revision as of 08:23, 10 September 2015

EF-Tu complexed with a GTP analog and the antibiotic GE2270 A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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