Elongation factor

spinqualitylabelsall models Structure of EF-Tu (grey and pink) with EF-Ts (green and yellow) (PDB entry 1efu) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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. 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. For EF-3 see HEAT Repeat For EF-SelB see SelB. 3D structures of elongation factor Updated on 24-November-2014 {"openlevels":0} EF-Tu 1efm, 1efc, 1dg1, 2fx3, 1etu – EcEF – Escherichia coli 1qzd – EcEF – Cryo EM 3u2q – EcEF + drug 1mj1 – EcEF + Phe-tRNA + S12 + S13 + L11 – Cryo EM 3ep2 - EcEF + tRNA + S12 + L11 + 16SRRNA + 23SRRNA – Cryo EM 1ttt, 1ob5 – TaEF + Phe-tRNA + GDPNP - Thermus aquaticus 1b23 - TaEF + Cys-tRNA 1ls2 – yEF + Phe-tRNA – yeast – Cryo EM 3agj – EF + plethora protein – Aeropyrum pernix 4h9g, 4lbv, 4lbw, 4lby, 4lbz, 4lc0 – TtEF – Thermus thermophilus 4j0q – EF – Pseudomonas putida EF-Tu complex with antibiotics 1ob2 - yEF + Phe-tRNA + antibiotic 4abr - TtEF + antibiotic in 30S ribosome 1ha3 - TtEF + antibiotic + GDP 2c77, 2c78 - TtEF + antibiotic + GTP analog 3fic, 3fic – TtEF + antibiotic in 70S ribosome – Cryo EM 2bvn - EcEF + GDP NP + antibiotic 1d8t, 2hcj, 2hdn, 3u6b, 3u6k, 4g5g – EcEF + antibiotic EF-Tu complex with nucleotide 1efu – EcEF + GDP 1exm – TtEF + GTP analog 1eft – TaEF + GNP – Thermus aquaticus 1tui – TaEF + GDP 1d2e – bEF + GDP – bovine 1jny, 1skq – SsEF + GDP – Sulfolobus solfataricus EF-Tu with EF-Ts 1efu – EcEF + EcEF-Ts 1aip - TtEF + TtEF-Ts - Thermus thermophilus 1xb2 – bEF + EF-Ts - bovine 1f60 – yEF + EF-Ts C terminal 1g7c - yEF + EF-Ts C terminal + GDPNP 1ije, 1ijf - yEF + EF-Ts C terminal + GDP 2b7b - yEF + EF-Ts C terminal (mutant) + GDP 2b7c - yEF + EF-Ts C terminal (mutant) EF-Tu in the ribosome 3eq3, 3eq4 – EcEF in 80S ribosome – Cryo EM 3izv, 3izw, 3fih - EcEF in 30S ribosome – Cryo EM 1zc8, 3dwu – TtEF in 70S ribosome – Cryo EM 2wrn, 2wrq, 2xqd, 2y0u, 2y0w, 2y0y, 2y10, 2y12, 2y14, 2y16, 2y18 - TtEF in 70S ribosome EF-SII 1tfi – hEF – human – NMR 3ndq - hEF domain II 1enw – yEF domain II – NMR 1eo0 - yEF domain I – NMR 2xex – SaEF – Staphylococcus aureus 1pqv, 1y1v – yEF + RNA polymerase II 1y1y, 3gtm – yEF + RNA polymerase II + RNA 1wjt – mEF N terminal – mouse – NMR 2m1h – EF PWWP domain – Trypanosoma brucei – NMR EF-ELL2 2e5n – hEF N2 domain - NMR EF-G 1efg, 1elo, 1ktv, 1wdt, 2dy1 – TtEF 1pn6, 3izp – TtEF – Cryo EM 4b8f, 4b8h – TtEF in 70S ribosome 4juw, 4kbt, 4kbv, 4kcy, 4kd0, 4kd8, 4kda, 4kdg, 4kdj, 4btc – TtEF in 30S ribosome 4kiy, 4kj0, 4kj2, 4kj4, 4kj6, 4kj8, 4kja, 4kjc – EcEF in 30S ribosome 3j5n – EcEF in 30S ribosome – Cryo-EM 3j5x – EcEF in 30S ribosome + antibiotics – Cryo-EM 1fnm, 2bm0, 2bm1 – TtEF (mutant) 2bcw – TtEF + L11 + L7/L12 2xex – SaEF 3zz0, 3zzt, 3zzu – SaEF (mutant) 2bv3 - TtEF (mutant) + GTP analog 2j7k - TtEF (mutant) + GDP analog 2om7, 2wri, 2wrk – TtEF in 70S ribosome – Cryo EM 2xsy, 2xuy - TtEF in 70S ribosome 1dar, 2efg – TtEF + GDP 1jqm, 1jqs – EcEF + L11 – Cryo EM 1zn0, 2rdo, 3j0e, 3j18 – EcEF in 30S ribosome – Cryo-EM 4fn5 – PaEF - Pseudomonas aeruginosa EF-GreA/GreB 2pn0 – EF – Nitrosomonas europaea 2p4v – EcEF-GreB 1grj – EcEF-GreA EF-NusA 1wcl, 1wcn – EcEF C terminal – NMR 2kwp - EcEF N terminal – NMR 2jzb – EcEF + RNA polymerase subunit α - NMR EF-P 1ueb – TtEF 3huw, 3huy – TtEF in 70S ribosome 3oyy – PaEF 3tre – EF – Coxiella burnetii 3a5z – EcEF + lysyl-tRNA synthetase EF-Ts 1tfe – TtEF 1b64 – hEF guanine exchange factor domain – NMR 2cp9 – UBA domain – NMR 1gh8 – EF – Methanobacterium thermoautotrophicum – NMR 2yy3 – EF – Pyrococcus horikoshii 2uz8 – hEF (mutant) EF-1G 1nhy – yEF N terminal 1pbu – hEF C terminal (mutant) - NMR EF-2 1n0v – yEF 1u2r – yEF + GDP 1n0u, 2e1r, 2npf – yEF + antifungal drug 1zm2, 1zm3, 1zm4, 1zm9, 3b78, 3b82, 3b8h, 2zit – yEF + exotoxin 1s1h - yEF + antifungal drug in 40S ribosome – Cryo EM 1s1h - hEF in 40S ribosome – Cryo EM 2p8w, 2p8x, 3dny - yEF in 80S ribosome – Cryo EM 2p8y, 2p8z - yEF+ antifungal drug in 80S ribosome – Cryo EM EF-3 2ix3 – yEF 2iwh – yEF + ADPNP 2iw3 – yEF + ADP 2ix8 – yEF in 80S ribosome – Cryo EM EF-SelB 1lva – MtEF C terminal – Moorella thermoacetica 2v9v – MtEF winged helix domain 1wsu, 2uwm – MtEF + RNA 2ply – MtEF (mutant) + RNA 1wb2, 4aca – MmEF – Methanococcus maripaludis 1wb3, 4acb – MmEF + GTP analog 4ac9, 1wb1 – MmEF + GDP 2pjp – EcEF + RNA EF-Spt5 2do3, 2e6z, 2e70 – hEF KOW motif – NMR 2exu – yEF 3h7h – hEF + hEF-Spt4 EF-Spt6 3gxw, 3gxx, 3pjp – EF SH2 domain – Candida glabrata 3psf, 3psi – yEF core domain 3psj, 3psk – yEF SH2 domain 2l3t - yEF SH2 domain]] - NMR 3oak – yEF + transcription factor IWS1 EF-CA150 2dod, 2doe, 2dof, 2e71, 2kiq, 2kis – hEF FF domain – NMR 3hfh – hEF FF domain 2ysi– mEF WW domain - NMR

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman