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| | <SX load='6tmf' size='340' side='right' viewer='molstar' caption='[[6tmf]], [[Resolution|resolution]] 2.80Å' scene=''> | | <SX load='6tmf' size='340' side='right' viewer='molstar' caption='[[6tmf]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6tmf]] is a 30 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermococcus_celer_dsm_2476 Thermococcus celer dsm 2476] and [http://en.wikipedia.org/wiki/Thermococcus_celer_vu_13_=_jcm_8558 Thermococcus celer vu 13 = jcm 8558]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TMF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TMF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6tmf]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_celer_Vu_13_=_JCM_8558 Thermococcus celer Vu 13 = JCM 8558]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TMF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TMF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SSOP1_0270, SULA_1305, SULB_1306, SULC_1304, SULG_06465, SULH_06465, SULI_06465, SULM_06465, SULN_06465, SULO_06475, SULZ_06710 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1293037 Thermococcus celer DSM 2476])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=6tmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tmf OCA], [http://pdbe.org/6tmf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tmf RCSB], [http://www.ebi.ac.uk/pdbsum/6tmf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tmf ProSAT]</span></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=6tmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tmf OCA], [https://pdbe.org/6tmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tmf RCSB], [https://www.ebi.ac.uk/pdbsum/6tmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tmf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A218P4M9_THECE A0A218P4M9_THECE]] Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.[HAMAP-Rule:MF_00531] [[http://www.uniprot.org/uniprot/A0A218P4N5_THECE A0A218P4N5_THECE]] With S4 and S12 plays an important role in translational accuracy.[HAMAP-Rule:MF_01307] [[http://www.uniprot.org/uniprot/A0A218NZW1_THECE A0A218NZW1_THECE]] Binds 16S rRNA, required for the assembly of 30S particles.[HAMAP-Rule:MF_01364] [[http://www.uniprot.org/uniprot/A0A218P4W7_THECE A0A218P4W7_THECE]] May be involved in maturation of the 30S ribosomal subunit.[HAMAP-Rule:MF_01474] [[http://www.uniprot.org/uniprot/A0A218NZT2_THECE A0A218NZT2_THECE]] Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement.[HAMAP-Rule:MF_01315] [[http://www.uniprot.org/uniprot/A0A218P3Q8_THECE A0A218P3Q8_THECE]] Involved in the binding of tRNA to the ribosomes.[HAMAP-Rule:MF_00508][SAAS:SAAS00243318] [[http://www.uniprot.org/uniprot/A0A218P167_THECE A0A218P167_THECE]] Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C'/D' sRNAs.[HAMAP-Rule:MF_00326] [[http://www.uniprot.org/uniprot/A0A218NZU7_THECE A0A218NZU7_THECE]] Binds the lower part of the 30S subunit head.[HAMAP-Rule:MF_01309] [[http://www.uniprot.org/uniprot/A0A218P4K4_THECE A0A218P4K4_THECE]] One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center.[HAMAP-Rule:MF_00480] [[http://www.uniprot.org/uniprot/A0A218NZU0_THECE A0A218NZU0_THECE]] Located on the platform of the 30S subunit.[HAMAP-Rule:MF_01310] [[http://www.uniprot.org/uniprot/A0A218P4I2_THECE A0A218P4I2_THECE]] With S4 and S5 plays an important role in translational accuracy. Located at the interface of the 30S and 50S subunits.[HAMAP-Rule:MF_00403][RuleBase:RU004490] [[http://www.uniprot.org/uniprot/A0A218NZX3_THECE A0A218NZX3_THECE]] One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.[HAMAP-Rule:MF_01345] [[http://www.uniprot.org/uniprot/A0A218NZT7_THECE A0A218NZT7_THECE]] One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.[HAMAP-Rule:MF_01302] [[http://www.uniprot.org/uniprot/A0A218NZV3_THECE A0A218NZV3_THECE]] One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.[HAMAP-Rule:MF_01306][SAAS:SAAS00896430] With S5 and S12 plays an important role in translational accuracy.[HAMAP-Rule:MF_01306][SAAS:SAAS00896433] | + | [https://www.uniprot.org/uniprot/A0A218NZR2_THECE A0A218NZR2_THECE] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6tmf" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6tmf" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[ATPase 3D structures|ATPase 3D structures]] |
| | + | *[[Ribosome 3D structures|Ribosome 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </SX> | | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thermococcus celer dsm 2476]] | + | [[Category: Thermococcus celer Vu 13 = JCM 8558]] |
| - | [[Category: Thermococcus celer vu 13 = jcm 8558]]
| + | [[Category: Becker T]] |
| - | [[Category: Becker, T]] | + | [[Category: Beckmann R]] |
| - | [[Category: Beckmann, R]] | + | [[Category: Kratzat H]] |
| - | [[Category: Kratzat, H]] | + | [[Category: Tampe R]] |
| - | [[Category: Tampe, R]] | + | |
| - | [[Category: Abc protein]]
| + | |
| - | [[Category: Ribosome]]
| + | |
| - | [[Category: Ribosome recycling]]
| + | |
| - | [[Category: Translation]]
| + | |
| Structural highlights
Function
A0A218NZR2_THECE
Publication Abstract from PubMed
Ribosome recycling by the twin-ATPase ABCE1 is a key regulatory process in mRNA translation and surveillance and in ribosome-associated protein quality control in Eukarya and Archaea. Here, we captured the archaeal 30S ribosome post-splitting complex at 2.8 A resolution by cryo-electron microscopy. The structure reveals the dynamic behavior of structural motifs unique to ABCE1, which ultimately leads to ribosome splitting. More specifically, we provide molecular details on how conformational rearrangements of the iron-sulfur cluster domain and hinge regions of ABCE1 are linked to closure of its nucleotide-binding sites. The combination of mutational and functional analyses uncovers an intricate allosteric network between the ribosome, regulatory domains of ABCE1, and its two structurally and functionally asymmetric ATP-binding sites. Based on these data, we propose a refined model of how signals from the ribosome are integrated into the ATPase cycle of ABCE1 to orchestrate ribosome recycling.
Molecular analysis of the ribosome recycling factor ABCE1 bound to the 30S post-splitting complex.,Nurenberg-Goloub E, Kratzat H, Heinemann H, Heuer A, Kotter P, Berninghausen O, Becker T, Tampe R, Beckmann R EMBO J. 2020 Feb 17:e103788. doi: 10.15252/embj.2019103788. PMID:32064661[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nurenberg-Goloub E, Kratzat H, Heinemann H, Heuer A, Kotter P, Berninghausen O, Becker T, Tampe R, Beckmann R. Molecular analysis of the ribosome recycling factor ABCE1 bound to the 30S post-splitting complex. EMBO J. 2020 Feb 17:e103788. doi: 10.15252/embj.2019103788. PMID:32064661 doi:http://dx.doi.org/10.15252/embj.2019103788
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