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4pc3

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Revision as of 13:30, 19 April 2017

Elongation factor Tu:Ts complex with partially bound GDP

Structural highlights

4pc3 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	4pc1, 4pc2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[EFTU1_ECOLI] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118] May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.[HAMAP-Rule:MF_00118] [EFTS_ECOLI] Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.[HAMAP-Rule:MF_00050]

Publication Abstract from PubMed

Translation elongation factor EF-Tu belongs to the superfamily of guanine-nucleotide binding proteins, which play key cellular roles as regulatory switches. All G-proteins require activation via exchange of GDP for GTP to carry out their respective tasks. Often, guanine-nucleotide exchange factors are essential to this process. During translation, EF-Tu:GTP transports aminoacylated tRNA to the ribosome. GTP is hydrolyzed during this process, and subsequent reactivation of EF-Tu is catalyzed by EF-Ts. The reaction path of guanine-nucleotide exchange is structurally poorly defined for EF-Tu and EF-Ts. We have determined the crystal structures of the following reaction intermediates: two structures of EF-Tu:GDP:EF-Ts (2.2 and 1.8A resolution), EF-Tu:PO4:EF-Ts (1.9A resolution), EF-Tu:GDPNP:EF-Ts (2.2A resolution) and EF-Tu:GDPNP:pulvomycin:Mg2+:EF-Ts (3.5A resolution). These structures provide snapshots throughout the entire exchange reaction and suggest a mechanism for the release of EF-Tu in its GTP conformation. An inferred sequence of events during the exchange reaction is presented.

Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu.,Thirup SS, Van LB, Nielsen TK, Knudsen CR J Struct Biol. 2015 Jun 11. pii: S1047-8477(15)30015-0. doi:, 10.1016/j.jsb.2015.06.011. PMID:26073967^[1]

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

References

↑ Thirup SS, Van LB, Nielsen TK, Knudsen CR. Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu. J Struct Biol. 2015 Jun 11. pii: S1047-8477(15)30015-0. doi:, 10.1016/j.jsb.2015.06.011. PMID:26073967 doi:http://dx.doi.org/10.1016/j.jsb.2015.06.011

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4pc3"

Categories: Thirup, S S | Elongation factor | G:gef:gdp complex | Protein synthesis | Translation

@@ Line 1: / Line 1: @@
 ==Elongation factor Tu:Ts complex with partially bound GDP==
 <StructureSection load='4pc3' size='340' side='right' caption='[[4pc3]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pc1|4pc1]], [[4pc2|4pc2]]</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=4pc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pc3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pc3 RCSB], [http://www.ebi.ac.uk/pdbsum/4pc3 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=4pc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pc3 OCA], [http://pdbe.org/4pc3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pc3 RCSB], [http://www.ebi.ac.uk/pdbsum/4pc3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pc3 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4pc3" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4pc3

From Proteopedia

Revision as of 13:30, 19 April 2017

Elongation factor Tu:Ts complex with partially bound GDP

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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