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| | <SX load='4cxh' size='340' side='right' viewer='molstar' caption='[[4cxh]], [[Resolution|resolution]] 8.90Å' scene=''> | | <SX load='4cxh' size='340' side='right' viewer='molstar' caption='[[4cxh]], [[Resolution|resolution]] 8.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4cxh]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CXH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4CXH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4cxh]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CXH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CXH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1MA:6-HYDRO-1-METHYLADENOSINE-5-MONOPHOSPHATE'>1MA</scene>, <scene name='pdbligand=2MG:2N-METHYLGUANOSINE-5-MONOPHOSPHATE'>2MG</scene>, <scene name='pdbligand=5MC:5-METHYLCYTIDINE-5-MONOPHOSPHATE'>5MC</scene>, <scene name='pdbligand=5MU:5-METHYLURIDINE+5-MONOPHOSPHATE'>5MU</scene>, <scene name='pdbligand=7MG:7N-METHYL-8-HYDROGUANOSINE-5-MONOPHOSPHATE'>7MG</scene>, <scene name='pdbligand=H2U:5,6-DIHYDROURIDINE-5-MONOPHOSPHATE'>H2U</scene>, <scene name='pdbligand=M2G:N2-DIMETHYLGUANOSINE-5-MONOPHOSPHATE'>M2G</scene>, <scene name='pdbligand=MIA:2-METHYLTHIO-N6-ISOPENTENYL-ADENOSINE-5-MONOPHOSPHATE'>MIA</scene>, <scene name='pdbligand=OMC:O2-METHYLYCYTIDINE-5-MONOPHOSPHATE'>OMC</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene>, <scene name='pdbligand=PSU:PSEUDOURIDINE-5-MONOPHOSPHATE'>PSU</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=1MA:6-HYDRO-1-METHYLADENOSINE-5-MONOPHOSPHATE'>1MA</scene>, <scene name='pdbligand=2MG:2N-METHYLGUANOSINE-5-MONOPHOSPHATE'>2MG</scene>, <scene name='pdbligand=5MC:5-METHYLCYTIDINE-5-MONOPHOSPHATE'>5MC</scene>, <scene name='pdbligand=5MU:5-METHYLURIDINE+5-MONOPHOSPHATE'>5MU</scene>, <scene name='pdbligand=7MG:7N-METHYL-8-HYDROGUANOSINE-5-MONOPHOSPHATE'>7MG</scene>, <scene name='pdbligand=H2U:5,6-DIHYDROURIDINE-5-MONOPHOSPHATE'>H2U</scene>, <scene name='pdbligand=M2G:N2-DIMETHYLGUANOSINE-5-MONOPHOSPHATE'>M2G</scene>, <scene name='pdbligand=MIA:2-METHYLTHIO-N6-ISOPENTENYL-ADENOSINE-5-MONOPHOSPHATE'>MIA</scene>, <scene name='pdbligand=OMC:O2-METHYLYCYTIDINE-5-MONOPHOSPHATE'>OMC</scene>, <scene name='pdbligand=PSU:PSEUDOURIDINE-5-MONOPHOSPHATE'>PSU</scene></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4cxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cxh OCA], [https://pdbe.org/4cxh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cxh RCSB], [https://www.ebi.ac.uk/pdbsum/4cxh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cxh ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cxb|4cxb]], [[4cxc|4cxc]], [[4cxd|4cxd]], [[4cxe|4cxe]], [[4cxg|4cxg]]</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=4cxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cxh OCA], [http://pdbe.org/4cxh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cxh RCSB], [http://www.ebi.ac.uk/pdbsum/4cxh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cxh ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/EF1A_AERPE EF1A_AERPE]] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis (By similarity). | + | [[https://www.uniprot.org/uniprot/EF1A_AERPE EF1A_AERPE]] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 27: |
Line 25: |
| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: European rabbit]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Oryctolagus cuniculus]] | | [[Category: Oryctolagus cuniculus]] |
| - | [[Category: Behrmann, E]] | + | [[Category: Behrmann E]] |
| - | [[Category: Budkevich, T V]] | + | [[Category: Budkevich TV]] |
| - | [[Category: Giesebrecht, J]] | + | [[Category: Giesebrecht J]] |
| - | [[Category: Hildebrand, P]] | + | [[Category: Hildebrand P]] |
| - | [[Category: Ismer, J]] | + | [[Category: Ismer J]] |
| - | [[Category: Loerke, J]] | + | [[Category: Loerke J]] |
| - | [[Category: Mielke, T]] | + | [[Category: Mielke T]] |
| - | [[Category: Nierhaus, K H]] | + | [[Category: Nierhaus KH]] |
| - | [[Category: Ramrath, D J.F]] | + | [[Category: Ramrath DJF]] |
| - | [[Category: Sanbonmatsu, K Y]] | + | [[Category: Sanbonmatsu KY]] |
| - | [[Category: Spahn, C M.T]] | + | [[Category: Spahn CMT]] |
| - | [[Category: Tung, C S]] | + | [[Category: Tung C-S]] |
| - | [[Category: Elongation cycle]]
| + | |
| - | [[Category: Elongation factor eef1a]]
| + | |
| - | [[Category: Eukaryotic ternary complex]]
| + | |
| - | [[Category: Mammalian 80s ribosome]]
| + | |
| - | [[Category: Translation]]
| + | |
| - | [[Category: Trna selection]]
| + | |
| Structural highlights
Function
[EF1A_AERPE] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis (By similarity).
Publication Abstract from PubMed
The extent to which bacterial ribosomes and the significantly larger eukaryotic ribosomes share the same mechanisms of ribosomal elongation is unknown. Here, we present subnanometer resolution cryoelectron microscopy maps of the mammalian 80S ribosome in the posttranslocational state and in complex with the eukaryotic eEF1AVal-tRNAGMPPNP ternary complex, revealing significant differences in the elongation mechanism between bacteria and mammals. Surprisingly, and in contrast to bacterial ribosomes, a rotation of the small subunit around its long axis and orthogonal to the well-known intersubunit rotation distinguishes the posttranslocational state from the classical pretranslocational state ribosome. We term this motion "subunit rolling." Correspondingly, a mammalian decoding complex visualized in substates before and after codon recognition reveals structural distinctions from the bacterial system. These findings suggest how codon recognition leads to GTPase activation in the mammalian system and demonstrate that in mammalia subunit rolling occurs during tRNA selection.
Regulation of the Mammalian elongation cycle by subunit rolling: a eukaryotic-specific ribosome rearrangement.,Budkevich TV, Giesebrecht J, Behrmann E, Loerke J, Ramrath DJ, Mielke T, Ismer J, Hildebrand PW, Tung CS, Nierhaus KH, Sanbonmatsu KY, Spahn CM Cell. 2014 Jul 3;158(1):121-31. doi: 10.1016/j.cell.2014.04.044. PMID:24995983[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Budkevich TV, Giesebrecht J, Behrmann E, Loerke J, Ramrath DJ, Mielke T, Ismer J, Hildebrand PW, Tung CS, Nierhaus KH, Sanbonmatsu KY, Spahn CM. Regulation of the Mammalian elongation cycle by subunit rolling: a eukaryotic-specific ribosome rearrangement. Cell. 2014 Jul 3;158(1):121-31. doi: 10.1016/j.cell.2014.04.044. PMID:24995983 doi:http://dx.doi.org/10.1016/j.cell.2014.04.044
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