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<StructureSection load='1efu' size='400' side='right' caption='Structure of EF-Tu with EF-Ts (PDB entry [[1efu]])' scene=''>
<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'>
__FORCETOC__


'''Elongation factors''' (EF) facilitate translational elongation during the formation of peptide bonds in the ribosome.  EF-selB is selenocysteine-specific EF.  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.
== Function ==
EF-Ts or EF 1-β (elongation factor thermo stable) catalyzes the release of GDP from EF-Tu.  EF-G translocates the peptidyl tRNA from the A site to the P site while moving the mRNA through the ribosome.  EF-SII helps RNA polymerase II to bypass blocks to elongation.  EF-ELL2 enhances polyadenylation and exon skipping with the gene encoding the immunoglobulin heavy-chain complex.  EF-GreA or GreB are cleavage factors allowing the resumption of elongation.  EF-NusA recruits translesion DNA polymerases to gaps encountered during translation.  EF-P alters the ribosome affinity to aminoacyl-tRNA.  EF-1 gamma acts during the delivery of aminoacyl tRNA to the ribosome.  EF-2 promotes the translocation of the nascent protein chain from the A site to the P site on the ribosome.  EF-3 is unique EF in fungi hence it provides an anti-fungal drug target. EF Spt4, Spt5, Spt6 are conserved among eukaryotes.  They modulate the chromatin structure.  EF-CA150 is believed to play a role in coupling transcription and splicing.  The elongin B and C complex is involved in the proteasomal degredation of target proteins.


==3D structures of elongation factor==
'''Elongation factors''' (EF) facilitate translational elongation during the formation of peptide bonds in the ribosome.<br />
* '''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-Ts or EF 1-β''' (elongation factor thermo stable) catalyzes the release of GDP from EF-Tu.<br />
* '''EF-G''' translocates the peptidyl tRNA from the A site to the P site while moving the mRNA through the ribosome.<br />
* '''EF-SII''' helps RNA polymerase II to bypass blocks to elongation.<br />
* '''EF-ELL2''' enhances polyadenylation and exon skipping with the gene encoding the immunoglobulin heavy-chain complex.<br />
* '''EF-GreA or GreB''' are cleavage factors allowing the resumption of elongation.<br />
* '''EF-NusA''' recruits translesion DNA polymerases to gaps encountered during translation.<br />
* '''EF-P''' alters the ribosome affinity to aminoacyl-tRNA.<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-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-CA150''' is believed to play a role in coupling transcription and splicing.<br />
*  '''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 />
* '''Negative EF''' (NELF) are involved in regulating the pausing of RNA Pol II polymerase transcripton<ref>PMID:38401543</ref>.<br />


===EF-Tu===
<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>


[[1efm]], [[1efc]], [[1dg1]], [[2fx3]] – EcEF – ''Escherichia coli''<BR />
==3D structures of elongation factor==
[[1qzd]] – EcEF – Cryo EM<BR />
[[Elongation factor 3D structures]]
[[3u2q]] – EcEF + drug<BR />
[[1mj1]] – EcEF + Phe-tRNA + S12 + S13 + L11 – Cryo EM<BR />
[[1ttt]], [[1ob5]] – TaEF + Phe-tRNA + GDPNP - ''Thermus aquaticus''<BR />
[[1b23]] - TaEF + Cys-tRNA<BR />
[[1ls2]] – yEF + Phe-tRNA – yeast – Cryo EM<BR />
[[3agj]] – EF + plethora protein – ''Aeropyrum pernix''


''EF-Tu complex with antibiotics''
</StructureSection>
 
[[1ob2]] - yEF + Phe-tRNA + antibiotic<BR />
[[4abr]] - TtEF + antibiotic in 30S ribosome<BR />
[[1ha3]] - TtEF + antibiotic + GDP<BR />
[[2c77]], [[2c78]] - TtEF + antibiotic + GTP analog<br />
[[3fic]], [[3fic]] – TtEF + antibiotic in 70S ribosome – Cryo EM<BR />
[[2bvn]] - EcEF + GDP<BR />NP + antibiotic<BR />
[[1d8t]], [[2hcj]], [[2hdn]], [[3u6b]], [[3u6k]] – EcEF + antibiotic


''EF-Tu complex with nucleotide''
== References ==
<references/>


[[1efu]] – EcEF + GDP<BR />
[[1exm]] – TtEF + GTP analog<br />
[[1eft]] – TaEF + GNP – ''Thermus aquaticus''<BR />
[[1tui]] – TaEF + GDP<BR />
[[1d2e]] – bEF + GDP – bovine<BR />
[[1jny]], [[1skq]] – SsEF + GDP – ''Sulfolobus solfataricus''
''EF-Tu with EF-Ts''
[[1efu]] – EcEF + EcEF-Ts<BR />
[[1aip]] - TtEF + TtEF-Ts - ''Thermus thermophilus''<BR />
[[1xb2]] – bEF + EF-Ts - bovine<BR />
[[1f60]]  – yEF + EF-Ts C terminal<BR />
[[1g7c]] - yEF + EF-Ts C terminal + GDPNP<BR />
[[1ije]], [[1ijf]] - yEF + EF-Ts C terminal + GDP<BR />
[[2b7b]] - yEF + EF-Ts C terminal (mutant) + GDP<BR />
[[2b7c]] - yEF + EF-Ts C terminal (mutant)
''EF-Tu in the ribosome''
[[3eq3]], [[3eq4]] – EcEF in 80S ribosome – Cryo EM<BR />
[[3izv]], [[3izw]] -  EcEF in 30S ribosome – Cryo EM<BR />
[[1zc8]], [[3dwu]] – TtEF in 70S ribosome – Cryo EM<BR />
[[2wrn]], [[2wrq]], [[2xqd]], [[2y0u]], [[2y0w]], [[2y0y]], [[2y10]], [[2y12]], [[2y14]], [[2y16]], [[2y18]] - TtEF in 70S ribosome
===EF-SII===
[[1tfi]] – hEF – human – NMR<BR />
[[3ndq]] - hEF domain II<BR />
[[1enw]] – yEF domain II – NMR<BR />
[[1eo0]] -  yEF domain I – NMR<BR />
[[2xex]] – SaEF – ''Staphylococcus aureus''<BR />
[[1pqv]], [[1y1v]] – yEF + RNA polymerase II<BR />
[[1y1y]], [[3gtm]] – yEF + RNA polymerase II + RNA<BR />
[[1wjt]] – mEF N terminal – mouse – NMR<BR />
===EF-ELL2===
[[2e5n]] – hEF N2 domain - NMR<BR />
===EF-G===
[[1efg]], [[1elo]], [[1ktv]], [[1wdt]], [[2dy1]] – TtEF<BR />
[[1pn6]], [[3izp]] – TtEF – Cryo EM<BR />
[[1fnm]], [[2bm0]], [[2bm1]] – TtEF (mutant) <BR />
[[2xex]] – SaEF<BR />
[[3zz0]], [[3zzt]], [[3zzu]] – SaEF (mutant) <BR />
[[2bv3]] - TtEF (mutant) + GTP analog<br />
[[2j7k]] - TtEF (mutant) + GDP analog<br />
[[2om7]], [[2wri]], [[2wrk]] – TtEF in 70S ribosome – Cryo EM<BR />
[[2xsy]], [[2xuy]] - TtEF in 70S ribosome<BR />
[[1dar]], [[2efg]] – TtEF + GDP<BR />
[[1jqm]], [[1jqs]] – EcEF + L11 – Cryo EM<BR />
[[1zn0]], [[2rdo]], [[3j0e]], [[3j18]] – EcEF in 30S ribosome – Cryo-EM<BR />
===EF-GreA/GreB===
[[2pn0]] – EF – ''Nitrosomonas europaea''<BR />
[[2p4v]] – EcEF-GreB
===EF-NusA===
[[1wcl]], [[1wcn]] – EcEF C terminal – NMR<BR />
[[2kwp]] - EcEF N terminal – NMR<BR />
[[2jzb]] – EcEF + RNA polymerase subunit α - NMR<BR />
===EF-P===
[[1ueb]] – TtEF<BR />
[[3huw]], [[3huy]] – TtEF in 70S ribosome<BR />
[[3oyy]] – EF – ''Pseudomonas aeruginosa''<BR />
[[3a5z]] – EcEF + lysyl-tRNA synthetase
===EF-Ts===
[[1tfe]] – TtEF<BR />
[[1b64]] – hEF guanine exchange factor domain – NMR<BR />
[[2cp9]] – UBA domain – NMR<BR />
[[1gh8]] – EF – ''Methanobacterium thermoautotrophicum'' – NMR<BR />
[[2yy3]] – EF – ''Pyrococcus horikoshii''<BR />
[[2uz8]] – hEF (mutant)
===EF-1G===
[[1nhy]] – yEF N terminal
[[1pbu]] – hEF C terminal (mutant) - NMR<BR />
===EF-2===
[[1n0v]] – yEF<BR />
[[1u2r]] – yEF + GDP<BR />
[[1n0u]], [[2e1r]], [[2npf]] – yEF + antifungal drug<BR />
[[1zm2]], [[1zm3]], [[1zm4]], [[1zm9]], [[3b78]], [[3b82]], [[3b8h]], [[2zit]] – yEF + exotoxin<BR />
[[1s1h]] - yEF + antifungal drug in 40S ribosome – Cryo EM<BR />
[[2p8w]], [[2p8x]], [[3dny]] - yEF in 80S ribosome – Cryo EM<BR />
[[2p8y]], [[2p8z]] - yEF+ antifungal drug in 80S ribosome – Cryo EM<BR />
===EF-3===
[[2ix3]] – yEF<BR />
[[2iwh]] – yEF + ADPNP<BR />
[[2iw3]] – yEF + ADP<BR />
[[2ix8]] – yEF in 80S ribosome – Cryo EM<BR />
===EF-SelB===
[[1lva]] – MtEF C terminal – ''Moorella thermoacetica''<BR />
[[2v9v]] – MtEF winged helix domain<BR />
[[1wsu]], [[2uwm]] – MtEF + RNA<BR />
[[2ply]] – MtEF (mutant) + RNA<BR />
[[1wb2]] – MmEF – ''Methanococcus maripaludis''<BR />
[[1wb3]] – MmEF + GTP analog<br />
[[4ac9]] – MmEF + GDP<BR />
[[2pjp]] – EcEF + RNA
===EF-Spt5===
[[2do3]], [[2e6z]], [[2e70]] – hEF KOW motif – NMR<BR />
[[2exu]] – yEF<BR />
[[3h7h]] – hEF + hEF-Spt4
===EF-Spt6===
[[3gxw]], [[3gxx]], [[3pjp]] – EF SH2 domain – ''Candida glabrata''<BR />
[[3psf]], [[3psi]] – yEF core domain<BR />
[[3psj]], [[3psk]] – yEF SH2 domain<BR />
[[2l3t]] - yEF SH2 domain]] - NMR<BR />
[[3oak]] – yEF + transcription factor IWS1
===EF-CA150===
[[2dod]], [[2doe]], [[2dof]], [[2e71]], [[2kiq]], [[2kis]] – hEF FF domain – NMR<BR />
[[3hfh]] – hEF FF domain<BR />
[[2ysi]]– mEF WW domain - NMR<BR />
===Elongin BC complex===
[[1lqb]] – hEloBC + von-Hippel Lindau disease tumor suppressor + hypoxia inducible factor 1 α<BR />
[[3zrc]], [[3ztc]], [[3ztd]], [[3zun]] - hEloBC + von-Hippel Lindau disease tumor suppressor + inhibitor<BR />
[[3zrf]] - hEloBC + von-Hippel Lindau disease tumor suppressor<BR />
[[2c9w]], [[2izv]], [[2jz3]] – hEloBC + suppressor of cytokine signaling<BR />
[[3dcg]] – hEloBC + virion infectivity factor<BR />
[[2xai]] - hEloBC + ankyrin repeat<BR />
[[2fnj]] - mEloBC + GUSTAVUS
</StructureSection>
[[Category:Topic Page]]
[[Category:Topic Page]]

Latest revision as of 08:35, 20 May 2025

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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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