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| * '''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 /> |
| * '''Elongin complex''' 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 /> | | * '''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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| <scene name='51/517376/Cv/2'>Complex EF-Tu with EF-Ts is heterotetramer</scene>, or, more exactly <scene name='51/517376/Cv/3'>heterodimer of homodimers</scene> (PDB entry [[1efu]]).<ref>PMID:8596629</ref> | | <scene name='51/517376/Cv/2'>Complex EF-Tu with EF-Ts is heterotetramer</scene>, or, more exactly <scene name='51/517376/Cv/3'>heterodimer of homodimers</scene> (PDB entry [[1efu]]).<ref>PMID:8596629</ref> |
Revision as of 16:24, 27 September 2018
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Elongation factors (EF) facilitate translational elongation during the formation of peptide bonds in the ribosome.
- EF-selB is selenocysteine-specific EF. See SelB
- 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[1].
- 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[2].
- EF-3 is a unique EF in fungi hence it provides an anti-fungal drug target. See HEAT Repeat
- 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 complex or SIII activates elongation by RNA polymerase II by suppressing transient pausing of the enzyme[3]. 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.
Complex EF-Tu with EF-Ts is heterotetramer, or, more exactly heterodimer of homodimers (PDB entry 1efu).[4]
- ↑ 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:https://dx.doi.org/10.1073/pnas.1006559107
- ↑ 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:https://dx.doi.org/10.1042/BST20060001
- ↑ 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
- ↑ 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:https://dx.doi.org/10.1038/379511a0
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3D structures of elongation factor
Updated on 27-September-2018
{"openlevels":0}
- EF-Tu
- SelB, HEAT Repeat, 1efu, 2fx3, 1etu, 5mi3 – EcEF – Escherichia coli
- 5mi8, 5mi9 – EcEF (mutant)
- 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
- 3wxm – ApEF + plethora protein – Aeropyrum pernix
- 4h9g, 4lbv, 4lbw, 4lby, 4lbz, 4lc0 – TtEF – Thermus thermophilus
- 4j0q – EF – Pseudomonas putida
- 5w75 – EF – Thermotoga neapolitana
- EF-Tu complex with antibiotics
- 1ob2 - yEF + Phe-tRNA + antibiotic
- 4v8q - TtEF + antibiotic in 30S ribosome
- 1ha3 - TtEF + antibiotic + GDP
- 2c77, 2c78 - TtEF + antibiotic + GTP analog
- 4v68 – TtEF + antibiotic in 70S ribosome – Cryo EM
- 2bvn - EcEF + GDP
NP + antibiotic
- 1d8t, 2hcj, 2hdn, 3u6b, 3u6k, 4g5g, 5jbq – 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
- 3wya – PhEF + GDP - Pyrococcus horikoshii
- EF-Tu complex with protein
- 3vmf – ApEF + translation termination factor
- 3wy9 – PhEF + L12
- 4p3y – EcEF + thiol:disulfide interchange protein
- 5i4r, 5i4q – EcEF + CDIA + CDII
- 4zv4 – PaEF + TSE6 - Pseudomonas aeruginosa
- EF-Tu with EF-Ts
- 1efu, 3agp, 3agq, 4pc1 – 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
- 4r71 – EcEF + EcEF-Ts + RNA polymerase β chain + S1
- 4pc7 – EcEF + EcEF-Ts + antibiotic + GNP
- 4pc2, 4pc3, 4pc6 – EcEF + EcEF-Ts + GDP derivative
- 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
- 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
- 5jw9 – hEF + AFF4 peptide
- EF-G
- 1efg, 1elo, 1ktv, 1wdt, 2dy1 – TtEF
- 4m1k, 4myt, 4myu – TtEF (mutant)
- 1pn6, 3izp – TtEF – 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
- 1dar, 2efg – TtEF + GDP
- 1jqm, 1jqs – EcEF + L11 – Cryo EM
- 4fn5 – PaEF
- 5tv2 – EF – Vibrio vulnificus
- 5ty0 – EF N terminal – Legionella pneumophila
- 5vh6 – EF N terminal – Bacillus subtilis
- 6b8d – EF N terminal – Haemophilus influenzae
- EF-G in the ribosome
- 4v8u, 4v5m, 4v5n – TtEF in 70S ribosome
- 4v9h, 4v9j, 4v9k, 4v9l, 4v9m, 4v90 – TtEF in 30S ribosome
- 4v9o, 4v9p – EcEF in 30S ribosome
- 4v9d – EcEF in 30S ribosome + antibiotics – Cryo-EM
- 2om7, 4v5f – TtEF in 70S ribosome – Cryo EM
- 1zn0, 2rdo, 3j0e, 4v6t, 4v9b – EcEF in 30S ribosome – Cryo-EM
- 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
- 4v6a – TtEF in 70S ribosome
- 3oyy – PaEF
- 3tre – EF – Coxiella burnetii
- 3a5z – EcEF + lysyl-tRNA synthetase
- 1yby – EF – Clostridium thermocellum
- 5j3b – EF – Acinetobacter baumannii
- 5wxk – EF + EARP – Neisseria meningitidis
- EF-Ts
- 1tfe – TtEF
- 1b64 – hEF guanine exchange factor domain – NMR
- 2cp9 – UBA domain – NMR
- 1gh8 – EF – Methanobacterium thermoautotrophicum – NMR
- 2yy3 – PhEF
- 2uz8 – hEF (mutant)
- EF-1
- 4c0s – rEF α-2 – rabbit
- 5dqs – hEF β+γ
- 5jpo – hEF γ+δ
- 1pbu – hEF γ C terminal (mutant) - NMR
- 2mvm, 2mvn – hEF δ-1 CAR domain – NMR
- 5o8w – yEF α+β
- 1nhy – yEF γ N terminal
- EF-2
- 1n0v – yEF
- 1u2r – yEF + GDP
- 1n0u, 2e1r, 2npf – yEF + antifungal drug
- 1zm2, 1zm3, 1zm4, 1zm9, 3b78, 3b82, 3b8h, 2zit – yEF + exotoxin
- 4v4b - 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
- 5h7j - PhEF
- 5h7l - PhEF + L12
- 5h7k - PhEF + GDP
- EF-3
- 2ix3 – yEF
- 2iwh – yEF + ADPNP
- 2iw3 – yEF + ADP
- 2ix8 – yEF in 80S ribosome – Cryo EM
- EF-4 (lepA)
- 2ywh, 2ywe, 2ywf, 2ywg - AalepA + nucleotide - Aquifex aeolicus
- 3cb4 - EclepA
- 3deg - EclepA in 70S ribosome + GMPPNP – Cryo EM
- EF-SelB
- 1lva – MtEF C terminal – Moorella thermoacetica
- 2v9v – MtEF winged helix domain
- 1wsu, 2uwm – MtEF + RNA
- 2ply – MtEF (mutant) + RNA
- 4zu9 - AaEF
- 4aca – MmEF – Methanococcus maripaludis
- 4acb – MmEF + GTP analog
- 4ac9 – MmEF + GDP
- 2pjp – EcEF + RNA
- 5izk, 5izl, 5izm – hEF + GDP derivative
- EF-Spt4 + EF-Spt5
- 5xon, 5xog – EF-Spt4 + EF-Spt5 + EF-Tfiis + RNA polymerase II - Komagataella phaffii - Cryo EM
- 5oik – bEF-Spt4 + EF-Spt5 + RNA polymerase II
- 2exu – yEF-Spt4 residues 1-99 + EF-Spt5 residues 285-375
- 3h7h – hEF-Spt4 residues 2-117 + hEF-Spt5 residues 176-273
- 4zn3, 4zn1 – EF-Spt4 + EF-Spt5 – Methanocaldococcus jannaschii
- EF-Spt5
- 2do3, 2e6z, 2e70 – hEF KOW motif residues 694-757 – NMR
- 5ohq – hEF KOW6-KOW7 domain residues 939-1087
- 5oho – hEF KOWX-KOW4 domain residues 536-646
- 4ytl – yEF KOW2-KOW3 domain residues 534-632
- 4ytk – yEF KOW1-linker domain residues 382-511
- 2exu – yEF
- EF-Spt6
- 3gxw, 3gxx, 3pjp – EF SH2 domain – Candida glabrata
- 3psf, 3psi – yEF core domain residues 235-1259
- 3psj, 3psk – yEF SH2 domain residues 1247-1451
- 5vkl, 5vko – yEF SH2 domain + RPB1 peptide
- 2l3t - yEF SH2 domain - NMR
- 3oak – yEF + transcription factor IWS1
- 4z2n – hEF middle domain residues 644-930
- 4z2m – hEF middle domain + histone H3.1 + histone H4
- EF-Spt16
- EF-M2-1
- 5nkx, 5noh – EF core domain – human respiratory cyncytial virus
- EF-TEFM mitochondrial
- 5ol9 - hEF N-terminal
- 5ol8 - hEF C-terminal
- 5ola - hEF + RNA polymerase + RNA + DNA
- EF-CA150
- Elongin A
- 4hfx – hEloA F-box domain
- Elongin BC complex
- 1lqb, 1lm8 – hEloBC + von-Hippel Lindau disease tumor suppressor + hypoxia inducible factor 1 α
- 3zrc, 3ztc, 3ztd, 3zun, 6fmi, 6fmj, 6fmk, 5nw2, 5nw1, 5nw0, 5nvz, 5nvy, 5nvx, 5nvw, 5nvv, 4w9l, 4w9k, 4w9j, 4w9i, 4w9h, 4w9g, 4w9f, 4w9e, 4w9d, 4w9c - hEloBC + von-Hippel Lindau disease tumor suppressor + inhibitor
- 5t35 - hEloBC + von-Hippel Lindau disease tumor suppressor + BRD4
- 4wqo - hEloBC + von-Hippel Lindau disease tumor suppressor + cullin-2
- 5n4w - hEloBC + von-Hippel Lindau disease tumor suppressor + cullin-2 + RBX1
- 3zrf, 5lli - hEloBC + von-Hippel Lindau disease tumor suppressor
- 2c9w, 2izv, 2jz3, 5bo4 – hEloBC + suppressor of cytokine signaling
- 6c5x – hEloBC + suppressor of cytokine signaling + Gp130 peptide
- 3dcg – hEloBC + virion infectivity factor
- 3zkj - hEloBC + ankyrin rep
- 1vcb – hEloBC + VHL
- 2fnj - mEloBC + GUSTAVUS
References
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