View source for 5mi8


==Structure of the phosphomimetic mutant of EF-Tu T383E==
<StructureSection load='5mi8' size='340' side='right'caption='[[5mi8]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5mi8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_HS Escherichia coli HS]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MI8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MI8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.18&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5mi8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mi8 OCA], [https://pdbe.org/5mi8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mi8 RCSB], [https://www.ebi.ac.uk/pdbsum/5mi8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mi8 ProSAT]</span></td></tr>
</table>
== Function ==
[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]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial protein synthesis is intricately connected to metabolic rate. One of the ways in which bacteria respond to environmental stress is through posttranslational modifications of translation factors. Translation elongation factor Tu (EF-Tu) is methylated and phosphorylated in response to nutrient starvation upon entering stationary phase, and its phosphorylation is a crucial step in the pathway toward sporulation. We analyze how phosphorylation leads to inactivation of Escherichia coli EF-Tu. We provide structural and biophysical evidence that phosphorylation of EF-Tu at T382 acts as an efficient switch that turns off protein synthesis by decoupling nucleotide binding from the EF-Tu conformational cycle. Direct modifications of the EF-Tu switch I region or modifications in other regions stabilizing the beta-hairpin state of switch I result in an effective allosteric trap that restricts the normal dynamics of EF-Tu and enables the evasion of the control exerted by nucleotides on G proteins. These results highlight stabilization of a phosphorylation-induced conformational trap as an essential mechanism for phosphoregulation of bacterial translation and metabolism. We propose that this mechanism may lead to the multisite phosphorylation state observed during dormancy and stationary phase.

Phosphorylation decelerates conformational dynamics in bacterial translation elongation factors.,Talavera A, Hendrix J, Versees W, Jurenas D, Van Nerom K, Vandenberk N, Singh RK, Konijnenberg A, De Gieter S, Castro-Roa D, Barth A, De Greve H, Sobott F, Hofkens J, Zenkin N, Loris R, Garcia-Pino A Sci Adv. 2018 Mar 14;4(3):eaap9714. doi: 10.1126/sciadv.aap9714. eCollection 2018, Mar. PMID:29546243<ref>PMID:29546243</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5mi8" style="background-color:#fffaf0;"></div>

==See Also==
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli HS]]
[[Category: Large Structures]]
[[Category: Barth A]]
[[Category: Castro-Roa D]]
[[Category: De Gieter S]]
[[Category: De Greve H]]
[[Category: Garcia-Pino A]]
[[Category: Hendrix J]]
[[Category: Hofkens J]]
[[Category: Jurenas D]]
[[Category: Loris R]]
[[Category: Talavera A]]
[[Category: Van Nerom K]]
[[Category: Vandenberk N]]
[[Category: Versees W]]
[[Category: Zenkin N]]