8j60: Difference between revisions
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==Structural and mechanistic insight into ribosomal ITS2 RNA processing by nuclease-kinase machinery== | |||
<StructureSection load='8j60' size='340' side='right'caption='[[8j60]], [[Resolution|resolution]] 3.39Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8j60]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cyberlindnera_jadinii Cyberlindnera jadinii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8J60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8J60 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.39Å</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=8j60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8j60 OCA], [https://pdbe.org/8j60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8j60 RCSB], [https://www.ebi.ac.uk/pdbsum/8j60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8j60 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Precursor ribosomal RNA (pre-rRNA) processing is a key step in ribosome biosynthesis and involves numerous RNases. A HEPN (higher eukaryote and prokaryote nucleotide binding) nuclease Las1 and a polynucleotide kinase Grc3 assemble into a tetramerase responsible for rRNA maturation. Here, we report the structures of full-length Saccharomyces cerevisiae and Cyberlindnera jadinii Las1-Grc3 complexes, and C. jadinii Las1. The Las1-Grc3 structures show that the central coiled-coil domain of Las1 facilitates pre-rRNA binding and cleavage, while the Grc3 C-terminal loop motif directly binds to the HEPN active center of Las1 and regulates pre-rRNA cleavage. Structural comparison between Las1 and Las1-Grc3 complex exhibits that Grc3 binding induces conformational rearrangements of catalytic residues associated with HEPN nuclease activation. Biochemical assays identify that Las1 processes pre-rRNA at the two specific sites (C2 and C2'), which greatly facilitates rRNA maturation. Our structures and specific pre-rRNA cleavage findings provide crucial insights into the mechanism and pathway of pre-rRNA processing in ribosome biosynthesis. | |||
Structural and mechanistic insights into ribosomal ITS2 RNA processing by nuclease-kinase machinery.,Chen J, Chen H, Li S, Lin X, Hu R, Zhang K, Liu L Elife. 2024 Jan 5;12:RP86847. doi: 10.7554/eLife.86847. PMID:38180340<ref>PMID:38180340</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8j60" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Cyberlindnera jadinii]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Chen H]] | |||
[[Category: Chen J]] | |||
[[Category: Hu R]] | |||
[[Category: Li S]] | |||
[[Category: Lin X]] | |||
[[Category: Liu L]] | |||
[[Category: Zhang K]] | |||
Latest revision as of 12:45, 17 October 2024
Structural and mechanistic insight into ribosomal ITS2 RNA processing by nuclease-kinase machineryStructural and mechanistic insight into ribosomal ITS2 RNA processing by nuclease-kinase machinery
Structural highlights
Publication Abstract from PubMedPrecursor ribosomal RNA (pre-rRNA) processing is a key step in ribosome biosynthesis and involves numerous RNases. A HEPN (higher eukaryote and prokaryote nucleotide binding) nuclease Las1 and a polynucleotide kinase Grc3 assemble into a tetramerase responsible for rRNA maturation. Here, we report the structures of full-length Saccharomyces cerevisiae and Cyberlindnera jadinii Las1-Grc3 complexes, and C. jadinii Las1. The Las1-Grc3 structures show that the central coiled-coil domain of Las1 facilitates pre-rRNA binding and cleavage, while the Grc3 C-terminal loop motif directly binds to the HEPN active center of Las1 and regulates pre-rRNA cleavage. Structural comparison between Las1 and Las1-Grc3 complex exhibits that Grc3 binding induces conformational rearrangements of catalytic residues associated with HEPN nuclease activation. Biochemical assays identify that Las1 processes pre-rRNA at the two specific sites (C2 and C2'), which greatly facilitates rRNA maturation. Our structures and specific pre-rRNA cleavage findings provide crucial insights into the mechanism and pathway of pre-rRNA processing in ribosome biosynthesis. Structural and mechanistic insights into ribosomal ITS2 RNA processing by nuclease-kinase machinery.,Chen J, Chen H, Li S, Lin X, Hu R, Zhang K, Liu L Elife. 2024 Jan 5;12:RP86847. doi: 10.7554/eLife.86847. PMID:38180340[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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