8c93: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8c93]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8C93 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8C93 FirstGlance]. <br> | <table><tr><td colspan='2'>[[8c93]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8C93 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8C93 FirstGlance]. <br> | ||
</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=8c93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8c93 OCA], [https://pdbe.org/8c93 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8c93 RCSB], [https://www.ebi.ac.uk/pdbsum/8c93 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8c93 ProSAT]</span></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]] 4.17Å</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=8c93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8c93 OCA], [https://pdbe.org/8c93 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8c93 RCSB], [https://www.ebi.ac.uk/pdbsum/8c93 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8c93 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 8c93" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 8c93" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ribosome 3D structures|Ribosome 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 09:50, 24 July 2024
Cryo-EM captures early ribosome assembly in actionCryo-EM captures early ribosome assembly in action
Structural highlights
FunctionRL3_ECOLI One of two assembly inititator proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.[HAMAP-Rule:MF_01325_B] Publication Abstract from PubMedRibosome biogenesis is a fundamental multi-step cellular process in all domains of life that involves the production, processing, folding, and modification of ribosomal RNAs (rRNAs) and ribosomal proteins. To obtain insights into the still unexplored early assembly phase of the bacterial 50S subunit, we exploited a minimal in vitro reconstitution system using purified ribosomal components and scalable reaction conditions. Time-limited assembly assays combined with cryo-EM analysis visualizes the structurally complex assembly pathway starting with a particle consisting of ordered density for only ~500 nucleotides of 23S rRNA domain I and three ribosomal proteins. In addition, our structural analysis reveals that early 50S assembly occurs in a domain-wise fashion, while late 50S assembly proceeds incrementally. Furthermore, we find that both ribosomal proteins and folded rRNA helices, occupying surface exposed regions on pre-50S particles, induce, or stabilize rRNA folds within adjacent regions, thereby creating cooperativity. Cryo-EM captures early ribosome assembly in action.,Qin B, Lauer SM, Balke A, Vieira-Vieira CH, Burger J, Mielke T, Selbach M, Scheerer P, Spahn CMT, Nikolay R Nat Commun. 2023 Feb 17;14(1):898. doi: 10.1038/s41467-023-36607-9. PMID:36797249[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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