Elongation factor: Difference between revisions
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For EF-3 see [[HEAT Repeat]]<br /> | For EF-3 see [[HEAT Repeat]]<br /> | ||
For EF-SelB see [[SelB]]. | For EF-SelB see [[SelB]]. | ||
==3D structures of elongation factor== | ==3D structures of elongation factor== | ||
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**[[1vcb]] – hEloBC + VHL<br /> | **[[1vcb]] – hEloBC + VHL<br /> | ||
**[[2fnj]] - mEloBC + GUSTAVUS | **[[2fnj]] - mEloBC + GUSTAVUS | ||
}} | }} | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 09:31, 29 March 2015
<StructureSection load='1efu' size='400' side='right' caption='Structure of EF-Tu (grey and pink) with EF-Ts (green and yellow) (PDB entry 1efu)' scene=>
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 γ 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 a 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.
- 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 29-March-2015 {{#tree:id=OrganizedByTopic|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 – ApEF + plethora protein – Aeropyrum pernix
- 4h9g, 4lbv, 4lbw, 4lby, 4lbz, 4lc0 – TtEF – Thermus thermophilus
- 4j0q – EF – Pseudomonas putida
- 1efm, 1efc, 1dg1, 2fx3, 1etu – EcEF – Escherichia coli
- EF-Tu complex with antibiotics
- EF-Tu complex with nucleotide
- EF-Tu complex with protein
- EF-Tu with EF-Ts
- 1efu, 3agp, 3agq – EcEF + EcEF-Ts
- 3avt, 3avu , 3avv, 3avw, 3avx, 3avy, 3vnu , 3vnv, 4fwt – EcEF + EcEF-Ts + RNA
- 3mmp – EcEF + EcEF-Ts + RNA replicase beta chain
- 4q7j – EcEF + EcEF-Ts + Q beta replicase + S1
- 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)
- 1efu, 3agp, 3agq – EcEF + EcEF-Ts
- EF-Tu in the ribosome
- EF-SII
- EF-ELL2
- 2e5n – hEF N2 domain - NMR
- 2e5n – hEF N2 domain - NMR
- EF-G
- 1efg, 1elo, 1ktv, 1wdt, 2dy1 – TtEF
- 4m1k, 4myt, 4myu – TtEF (mutant)
- 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
- 1efg, 1elo, 1ktv, 1wdt, 2dy1 – TtEF
- EF-GreA/GreB
- EF-NusA
- EF-P
- EF-Ts
- EF-1 α-2
- 4c0s – rEF – rabbit
- 4c0s – rEF – rabbit
- EF-1 δ-1
- EF-1G
- EF-2
- 1n0v – yEF
- 1u2r – yEF + GDP
- 1n0u, 2e1r, 2npf – yEF + antifungal drug
- 1zm2, 1zm3, 1zm4, 1zm9, 3b78, 3b82, 3b8h, 2zit – yEF + exotoxin
- 1s1h - hEF in 40S ribosome – Cryo EM
- 4cxg, 4cxh - rEF in 40S ribosome – Cryo EM
- 2p8w, 2p8x, 3dny - yEF in 80S ribosome – Cryo EM
- 2p8y, 2p8z - yEF+ antifungal drug in 80S ribosome – Cryo EM
- 1n0v – yEF
- EF-3
- EF-4 (lepA)
- EF-SelB
- EF-Spt5
- EF-Spt6
- EF-CA150
- Elongin BC complex
- 1lqb, 1lm8 – hEloBC + von-Hippel Lindau disease tumor suppressor + hypoxia inducible factor 1 α
- 3zrc, 3ztc, 3ztd, 3zun - hEloBC + von-Hippel Lindau disease tumor suppressor + inhibitor
- 3zrf - hEloBC + von-Hippel Lindau disease tumor suppressor
- 2c9w, 2izv, [[2jz3 – hEloBC + suppressor of cytokine signaling
- 3dcg – hEloBC + virion infectivity factor
- 2xai - hEloBC + ankyrin rep
- 1vcb – hEloBC + VHL
- 2fnj - mEloBC + GUSTAVUS
- 1lqb, 1lm8 – hEloBC + von-Hippel Lindau disease tumor suppressor + hypoxia inducible factor 1 α
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