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4pc3

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'''Unreleased structure'''
 
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The entry 4pc3 is ON HOLD until Paper Publication
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==Elongation factor Tu:Ts complex with partially bound GDP==
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<StructureSection load='4pc3' size='340' side='right'caption='[[4pc3]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4pc3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PC3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PC3 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8313&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4pc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pc3 OCA], [https://pdbe.org/4pc3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pc3 RCSB], [https://www.ebi.ac.uk/pdbsum/4pc3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pc3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/EFTU1_ECOLI 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]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Thirup, S.S.
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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<ref>PMID:26073967</ref>
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Description: Elongation factor Tu:Ts complex with partially bound GDP
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4pc3" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Elongation factor 3D structures|Elongation factor 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli K-12]]
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[[Category: Large Structures]]
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[[Category: Thirup SS]]

Current revision

Elongation factor Tu:Ts complex with partially bound GDP

PDB ID 4pc3

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