Elongation factor

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<StructureSection load='1efu' size='350' side='right' caption='Structure of EF-Tu (grey and pink) with EF-Ts (green and yellow) (PDB entry [[1efu]])' scene=''>
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<StructureSection load='' size='350' side='right' caption='Structure of EF-Tu (cyan and magenta) with EF-Ts (green and yellow) (PDB entry [[1efu]])' scene='51/517376/Cv/1'>
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__FORCETOC__
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== Function ==
'''Elongation factors''' (EF) facilitate translational elongation during the formation of peptide bonds in the ribosome.<br />
'''Elongation factors''' (EF) facilitate translational elongation during the formation of peptide bonds in the ribosome.<br />
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* '''EF-selB''' is selenocysteine-specific EF.<br />
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* '''EF-selB''' is selenocysteine-specific EF. See [[SelB]]<br />
* '''EF-Tu or EF 1-α''' (elongation factor thermo unstable) is a prokaryotic EF. EF-Tu contributes to translational accuracy. It catalyzes the addition of aminoacyl tRNA<ref>PMID:20798060</ref>. <br />
* '''EF-Tu or EF 1-α''' (elongation factor thermo unstable) is a prokaryotic EF. EF-Tu contributes to translational accuracy. It catalyzes the addition of aminoacyl tRNA<ref>PMID:20798060</ref>. <br />
*'''EF-Ts or EF 1-β''' (elongation factor thermo stable) catalyzes the release of GDP from EF-Tu.<br />
*'''EF-Ts or EF 1-β''' (elongation factor thermo stable) catalyzes the release of GDP from EF-Tu.<br />
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* '''EF-1 γ''' acts during the delivery of aminoacyl tRNA to the ribosome.<br />
* '''EF-1 γ''' acts during the delivery of aminoacyl tRNA to the ribosome.<br />
* '''EF-2''' promotes the translocation of the nascent protein chain from the A site to the P site on the ribosome<ref>PMID:16246167</ref>.<br />
* '''EF-2''' promotes the translocation of the nascent protein chain from the A site to the P site on the ribosome<ref>PMID:16246167</ref>.<br />
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* '''EF-3''' is a unique EF in fungi hence it provides an anti-fungal drug target.<br />
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* '''EF-3''' is a unique EF in fungi hence it provides an anti-fungal drug target. See [[HEAT Repeat]]<br />
* '''EF Spt4, Spt5, Spt6''' are conserved among eukaryotes. They modulate the chromatin structure.<br />
* '''EF Spt4, Spt5, Spt6''' are conserved among eukaryotes. They modulate the chromatin structure.<br />
* '''EF-CA150''' is believed to play a role in coupling transcription and splicing.<br />
* '''EF-CA150''' is believed to play a role in coupling transcription and splicing.<br />
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* '''Elongin B and C complex''' is involved in the proteasomal degredation of target proteins.<br />
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* '''Elongin complex''' or '''SIII''' activates elongation by RNA polymerase II by suppressing transient pausing of the enzyme<ref>PMID:7660129</ref>. The complex is composed of elongin A, B and C. '''Elongin A''' (EloA) is the active component of the complex. '''Elongin B and C''' (EloBC) are the regulatory subunits of it. '''Von Hippel-Landau tumor suppressor protein''' (VHL) binds to EloBC and inhibits transcriptional elongation.<br />
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For EF-3 see [[HEAT Repeat]]<br />
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* '''Negative EF''' (NELF) are involved in regulating the pausing of RNA Pol II polymerase transcripton<ref>PMID:38401543</ref>.<br />
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For EF-SelB see [[SelB]].
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</StructureSection>
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<scene name='51/517376/Cv/4'>Complex EF-Tu with EF-Ts is heterotetramer</scene>, or, more exactly <scene name='51/517376/Cv/5'>heterodimer of homodimers</scene> (PDB entry [[1efu]]).<ref>PMID:8596629</ref>
==3D structures of elongation factor==
==3D structures of elongation factor==
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[[Elongation factor 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*EF-Tu
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**[[1efm]], [[1efc]], [[1dg1]], [[2fx3]], [[1etu]] – EcEF – ''Escherichia coli''<BR />
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**[[1qzd]] – EcEF – Cryo EM<BR />
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**[[3u2q]] – EcEF + drug<BR />
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**[[1mj1]] – EcEF + Phe-tRNA + S12 + S13 + L11 – Cryo EM<BR />
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**[[3ep2]] - EcEF + tRNA + S12 + L11 + 16SRRNA + 23SRRNA – Cryo EM<BR />
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**[[1ttt]], [[1ob5]] – TaEF + Phe-tRNA + GDPNP - ''Thermus aquaticus''<BR />
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**[[1b23]] - TaEF + Cys-tRNA<BR />
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**[[1ls2]] – yEF + Phe-tRNA – yeast – Cryo EM<BR />
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**[[3agj]] – ApEF + plethora protein – ''Aeropyrum pernix''<br />
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**[[4h9g]], [[4lbv]], [[4lbw]], [[4lby]], [[4lbz]], [[4lc0]] – TtEF – ''Thermus thermophilus''<br />
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**[[4j0q]] – EF – ''Pseudomonas putida''<br />
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*''EF-Tu complex with antibiotics''
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**[[1ob2]] - yEF + Phe-tRNA + antibiotic<BR />
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**[[4abr]] - TtEF + antibiotic in 30S ribosome<BR />
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**[[1ha3]] - TtEF + antibiotic + GDP<BR />
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**[[2c77]], [[2c78]] - TtEF + antibiotic + GTP analog<br />
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**[[3fic]], [[3fic]] – TtEF + antibiotic in 70S ribosome – Cryo EM<BR />
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**[[2bvn]] - EcEF + GDP<BR />NP + antibiotic<BR />
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**[[1d8t]], [[2hcj]], [[2hdn]], [[3u6b]], [[3u6k]], [[4g5g]] – EcEF + antibiotic
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*''EF-Tu complex with nucleotide''
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**[[1efu]] – EcEF + GDP<BR />
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**[[1exm]] – TtEF + GTP analog<br />
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**[[1eft]] – TaEF + GNP – ''Thermus aquaticus''<BR />
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**[[1tui]] – TaEF + GDP<BR />
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**[[1d2e]] – bEF + GDP – bovine<BR />
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**[[1jny]], [[1skq]] – SsEF + GDP – ''Sulfolobus solfataricus''<br />
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**[[3wya]] – PhEF + GDP - ''Pyrococcus horikoshii''<br />
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*''EF-Tu complex with protein''
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**[[3vmf]] – ApEF + translation termination factor<br />
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**[[3wxm]] – ApEF + protein pelota homolog<br />
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**[[3wy9]] – PhEF + L12 <br />
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**[[4p3y]] – EcEF + thiol:disulfide interchange protein <br />
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*''EF-Tu with EF-Ts''
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**[[1efu]], [[3agp]], [[3agq]] – EcEF + EcEF-Ts<BR />
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**[[3avt]], [[3avu]] , [[3avv]], [[3avw]], [[3avx]], [[3avy]], [[3vnu]] , [[3vnv]], [[4fwt]] – EcEF + EcEF-Ts + RNA<br />
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**[[3mmp]] – EcEF + EcEF-Ts + RNA replicase beta chain<br />
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**[[4q7j]] – EcEF + EcEF-Ts + Q beta replicase + S1<br />
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**[[1aip]] - TtEF + TtEF-Ts - ''Thermus thermophilus''<BR />
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**[[1xb2]] – bEF + EF-Ts - bovine<BR />
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**[[1f60]] – yEF + EF-Ts C terminal<BR />
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**[[1g7c]] - yEF + EF-Ts C terminal + GDPNP<BR />
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**[[1ije]], [[1ijf]] - yEF + EF-Ts C terminal + GDP<BR />
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**[[2b7b]] - yEF + EF-Ts C terminal (mutant) + GDP<BR />
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**[[2b7c]] - yEF + EF-Ts C terminal (mutant)
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*''EF-Tu in the ribosome''
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**[[3eq3]], [[3eq4]] – EcEF in 80S ribosome – Cryo EM<BR />
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**[[3izv]], [[3izw]], [[3fih]] - EcEF in 30S ribosome – Cryo EM<BR />
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**[[1zc8]], [[3dwu]] – TtEF in 70S ribosome – Cryo EM<BR />
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**[[2wrn]], [[2wrq]], [[2xqd]], [[2y0u]], [[2y0w]], [[2y0y]], [[2y10]], [[2y12]], [[2y14]], [[2y16]], [[2y18]] - TtEF in 70S ribosome
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*EF-SII
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**[[1tfi]] – hEF – human – NMR<BR />
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**[[3ndq]] - hEF domain II<BR />
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**[[1enw]] – yEF domain II – NMR<BR />
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**[[1eo0]] - yEF domain I – NMR<BR />
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**[[2xex]] – SaEF – ''Staphylococcus aureus''<BR />
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**[[1pqv]], [[1y1v]] – yEF + RNA polymerase II<BR />
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**[[1y1y]], [[3gtm]] – yEF + RNA polymerase II + RNA<BR />
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**[[1wjt]] – mEF N terminal – mouse – NMR<BR />
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**[[2m1h]] – EF PWWP domain – ''Trypanosoma brucei'' – NMR<br />
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*EF-ELL2
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**[[2e5n]] – hEF N2 domain - NMR<BR />
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*EF-G
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**[[1efg]], [[1elo]], [[1ktv]], [[1wdt]], [[2dy1]] – TtEF<BR />
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**[[4m1k]], [[4myt]], [[4myu]] – TtEF (mutant)<br />
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**[[1pn6]], [[3izp]] – TtEF – Cryo EM<BR />
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**[[4b8f]], [[4b8h]] – TtEF in 70S ribosome <BR />
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**[[4juw]], [[4kbt]], [[4kbv]], [[4kcy]], [[4kd0]], [[4kd8]], [[4kda]], [[4kdg]], [[4kdj]], [[4btc]] – TtEF in 30S ribosome <BR />
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**[[4kiy]], [[4kj0]], [[4kj2]], [[4kj4]], [[4kj6]], [[4kj8]], [[4kja]], [[4kjc]] – EcEF in 30S ribosome <BR />
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**[[3j5n]] – EcEF in 30S ribosome – Cryo-EM<BR />
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**[[3j5x]] – EcEF in 30S ribosome + antibiotics – Cryo-EM<BR />
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**[[1fnm]], [[2bm0]], [[2bm1]] – TtEF (mutant) <BR />
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**[[2bcw]] – TtEF + L11 + L7/L12 <br />
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**[[2xex]] – SaEF<BR />
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**[[3zz0]], [[3zzt]], [[3zzu]] – SaEF (mutant) <BR />
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**[[2bv3]] - TtEF (mutant) + GTP analog<br />
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**[[2j7k]] - TtEF (mutant) + GDP analog<br />
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**[[2om7]], [[2wri]], [[2wrk]] – TtEF in 70S ribosome – Cryo EM<BR />
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**[[2xsy]], [[2xuy]] - TtEF in 70S ribosome<BR />
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**[[1dar]], [[2efg]] – TtEF + GDP<BR />
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**[[1jqm]], [[1jqs]] – EcEF + L11 – Cryo EM<BR />
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**[[1zn0]], [[2rdo]], [[3j0e]], [[3j18]] – EcEF in 30S ribosome – Cryo-EM<BR />
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**[[4fn5]] – PaEF - ''Pseudomonas aeruginosa''<br />
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*EF-GreA/GreB
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**[[2pn0]] – EF – ''Nitrosomonas europaea''<BR />
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**[[2p4v]] – EcEF-GreB<br />
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**[[1grj]] – EcEF-GreA<br />
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*EF-NusA
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**[[1wcl]], [[1wcn]] – EcEF C terminal – NMR<BR />
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**[[2kwp]] - EcEF N terminal – NMR<BR />
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**[[2jzb]] – EcEF + RNA polymerase subunit α - NMR<BR />
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*EF-P
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**[[1ueb]] – TtEF<BR />
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**[[3huw]], [[3huy]] – TtEF in 70S ribosome<BR />
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**[[3oyy]] – PaEF <BR />
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**[[3tre]] – EF – ''Coxiella burnetii''<br />
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**[[3a5z]] – EcEF + lysyl-tRNA synthetase<br />
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**[[1yby]] – EF – ''Clostridium thermocellum''<br />
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*EF-Ts
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**[[1tfe]] – TtEF<BR />
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**[[1b64]] – hEF guanine exchange factor domain – NMR<BR />
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**[[2cp9]] – UBA domain – NMR<BR />
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**[[1gh8]] – EF – ''Methanobacterium thermoautotrophicum'' – NMR<BR />
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**[[2yy3]] – PhEF <BR />
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**[[2uz8]] – hEF (mutant)
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*EF-1 α-2
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**[[4c0s]] – rEF – rabbit<br />
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*EF-1 δ-1
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**[[2mvm]], [[2mvn]] – hEF CAR domain – NMR<br />
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*EF-1G
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**[[1nhy]] – yEF N terminal
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**[[1pbu]] – hEF C terminal (mutant) - NMR<BR />
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*EF-2
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**[[1n0v]] – yEF<BR />
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**[[1u2r]] – yEF + GDP<BR />
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**[[1n0u]], [[2e1r]], [[2npf]] – yEF + antifungal drug<BR />
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**[[1zm2]], [[1zm3]], [[1zm4]], [[1zm9]], [[3b78]], [[3b82]], [[3b8h]], [[2zit]] – yEF + exotoxin<BR />
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**[[1s1h]] - hEF in 40S ribosome – Cryo EM<BR />
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**[[4cxg]], [[4cxh]] - rEF in 40S ribosome – Cryo EM<BR />
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**[[2p8w]], [[2p8x]], [[3dny]] - yEF in 80S ribosome – Cryo EM<BR />
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**[[2p8y]], [[2p8z]] - yEF+ antifungal drug in 80S ribosome – Cryo EM<BR />
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*EF-3
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**[[2ix3]] – yEF<BR />
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**[[2iwh]] – yEF + ADPNP<BR />
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**[[2iw3]] – yEF + ADP<BR />
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**[[2ix8]] – yEF in 80S ribosome – Cryo EM<BR />
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*EF-4 (lepA)
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**[[2ywh]], [[2ywe]], [[2ywf]], [[2ywg]] - AalepA + nucleotide - ''Aquifex aeolicus''<BR />
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**[[3cb4]] - EclepA <BR />
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**[[3deg]] - EclepA in 70S ribosome + GMPPNP – Cryo EM<BR />
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*EF-SelB
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**[[1lva]] – MtEF C terminal – ''Moorella thermoacetica''<BR />
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**[[2v9v]] – MtEF winged helix domain<BR />
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**[[1wsu]], [[2uwm]] – MtEF + RNA<BR />
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**[[2ply]] – MtEF (mutant) + RNA<BR />
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**[[1wb2]], [[4aca]] – MmEF – ''Methanococcus maripaludis''<BR />
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**[[1wb3]], [[4acb]] – MmEF + GTP analog<br />
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**[[4ac9]], [[1wb1]] – MmEF + GDP<BR />
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**[[2pjp]] – EcEF + RNA
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*EF-Spt5
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**[[2do3]], [[2e6z]], [[2e70]] – hEF KOW motif – NMR<BR />
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**[[2exu]] – yEF<BR />
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**[[3h7h]] – hEF + hEF-Spt4
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*EF-Spt6
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**[[3gxw]], [[3gxx]], [[3pjp]] – EF SH2 domain – ''Candida glabrata''<BR />
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**[[3psf]], [[3psi]] – yEF core domain<BR />
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**[[3psj]], [[3psk]] – yEF SH2 domain<BR />
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**[[2l3t]] - yEF SH2 domain]] - NMR<BR />
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**[[3oak]] – yEF + transcription factor IWS1
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*EF-CA150
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**[[2dod]], [[2doe]], [[2dof]], [[2e71]], [[2kiq]], [[2kis]] – hEF FF domain – NMR<BR />
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**[[3hfh]] – hEF FF domain<BR />
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**[[2ysi]]– mEF WW domain - NMR<BR />
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*Elongin BC complex
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**[[1lqb]], [[1lm8]] – hEloBC + von-Hippel Lindau disease tumor suppressor + hypoxia inducible factor 1 α<br />
 
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**[[3zrc]], [[3ztc]], [[3ztd]], [[3zun]] - hEloBC + von-Hippel Lindau disease tumor suppressor + inhibitor<br />
 
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**[[3zrf]] - hEloBC + von-Hippel Lindau disease tumor suppressor<br />
 
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**[[2c9w]], [[2izv]], [[2jz3]] – hEloBC + suppressor of cytokine signaling<br />
 
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**[[3dcg]] – hEloBC + virion infectivity factor<br />
 
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**[[2xai]] - hEloBC + ankyrin rep<br />
 
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**[[1vcb]] – hEloBC + VHL<br />
 
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**[[2fnj]] - mEloBC + GUSTAVUS
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Structure of EF-Tu (cyan and magenta) with EF-Ts (green and yellow) (PDB entry 1efu)

Drag the structure with the mouse to rotate

References

  1. ↑ Takeshita D, Tomita K. Assembly of Q{beta} viral RNA polymerase with host translational elongation factors EF-Tu and -Ts. Proc Natl Acad Sci U S A. 2010 Sep 7;107(36):15733-8. Epub 2010 Aug 23. PMID:20798060 doi:http://dx.doi.org/10.1073/pnas.1006559107
  2. ↑ Jorgensen R, Merrill AR, Andersen GR. The life and death of translation elongation factor 2. Biochem Soc Trans. 2006 Feb;34(Pt 1):1-6. PMID:16246167 doi:http://dx.doi.org/10.1042/BST20060001
  3. ↑ Aso T, Lane WS, Conaway JW, Conaway RC. Elongin (SIII): a multisubunit regulator of elongation by RNA polymerase II. Science. 1995 Sep 8;269(5229):1439-43. PMID:7660129
  4. ↑ Su BG, Vos SM. Distinct negative elongation factor conformations regulate RNA polymerase II promoter-proximal pausing. Mol Cell. 2024 Apr 4;84(7):1243-1256.e5. PMID:38401543 doi:10.1016/j.molcel.2024.01.023
  5. ↑ Kawashima T, Berthet-Colominas C, Wulff M, Cusack S, Leberman R. The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution. Nature. 1996 Feb 8;379(6565):511-8. PMID:8596629 doi:http://dx.doi.org/10.1038/379511a0

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