8fmw: Difference between revisions
New page: '''Unreleased structure''' The entry 8fmw is ON HOLD Authors: Description: Category: Unreleased Structures |
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The | ==The structure of a hibernating ribosome in the Lyme disease pathogen== | ||
<StructureSection load='8fmw' size='340' side='right'caption='[[8fmw]], [[Resolution|resolution]] 2.86Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8fmw]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Borreliella_burgdorferi_B31 Borreliella burgdorferi B31]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FMW 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]] 2.86Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=8fmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fmw OCA], [https://pdbe.org/8fmw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fmw RCSB], [https://www.ebi.ac.uk/pdbsum/8fmw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fmw ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RL15_BORBU RL15_BORBU] Binds to the 23S rRNA.[HAMAP-Rule:MF_01341] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The spirochete bacterial pathogen Borrelia (Borreliella) burgdorferi (Bbu) affects more than 10% of the world population and causes Lyme disease in about half a million people in the US annually. Therapy for Lyme disease includes antibiotics that target the Bbu ribosome. Here we present the structure of the Bbu 70S ribosome obtained by single particle cryo-electron microscopy at 2.9 A resolution, revealing a bound hibernation promotion factor protein and two genetically non-annotated ribosomal proteins bS22 and bL38. The ribosomal protein uL30 in Bbu has an N-terminal alpha-helical extension, partly resembling the mycobacterial bL37 protein, suggesting evolution of bL37 and a shorter uL30 from a longer uL30 protein. Its analogy to proteins uL30m and mL63 in mammalian mitochondrial ribosomes also suggests a plausible evolutionary pathway for expansion of protein content in mammalian mitochondrial ribosomes. Computational binding free energy predictions for antibiotics reflect subtle distinctions in antibiotic-binding sites in the Bbu ribosome. Discovery of these features in the Bbu ribosome may enable better ribosome-targeted antibiotic design for Lyme disease treatment. | |||
The structure of a hibernating ribosome in a Lyme disease pathogen.,Sharma MR, Manjari SR, Agrawal EK, Keshavan P, Koripella RK, Majumdar S, Marcinkiewicz AL, Lin YP, Agrawal RK, Banavali NK Nat Commun. 2023 Oct 31;14(1):6961. doi: 10.1038/s41467-023-42266-7. PMID:37907464<ref>PMID:37907464</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8fmw" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Borreliella burgdorferi B31]] | |||
[[Category: Large Structures]] | |||
[[Category: Agrawal EK]] | |||
[[Category: Agrawal RK]] | |||
[[Category: Banavali NK]] | |||
[[Category: Keshavan P]] | |||
[[Category: Koripella RK]] | |||
[[Category: Lin YP]] | |||
[[Category: Majumdar S]] | |||
[[Category: Manjari SR]] | |||
[[Category: Marcinkiewicz AL]] | |||
[[Category: Sharma MR]] | |||
Latest revision as of 10:15, 21 November 2024
The structure of a hibernating ribosome in the Lyme disease pathogenThe structure of a hibernating ribosome in the Lyme disease pathogen
Structural highlights
FunctionRL15_BORBU Binds to the 23S rRNA.[HAMAP-Rule:MF_01341] Publication Abstract from PubMedThe spirochete bacterial pathogen Borrelia (Borreliella) burgdorferi (Bbu) affects more than 10% of the world population and causes Lyme disease in about half a million people in the US annually. Therapy for Lyme disease includes antibiotics that target the Bbu ribosome. Here we present the structure of the Bbu 70S ribosome obtained by single particle cryo-electron microscopy at 2.9 A resolution, revealing a bound hibernation promotion factor protein and two genetically non-annotated ribosomal proteins bS22 and bL38. The ribosomal protein uL30 in Bbu has an N-terminal alpha-helical extension, partly resembling the mycobacterial bL37 protein, suggesting evolution of bL37 and a shorter uL30 from a longer uL30 protein. Its analogy to proteins uL30m and mL63 in mammalian mitochondrial ribosomes also suggests a plausible evolutionary pathway for expansion of protein content in mammalian mitochondrial ribosomes. Computational binding free energy predictions for antibiotics reflect subtle distinctions in antibiotic-binding sites in the Bbu ribosome. Discovery of these features in the Bbu ribosome may enable better ribosome-targeted antibiotic design for Lyme disease treatment. The structure of a hibernating ribosome in a Lyme disease pathogen.,Sharma MR, Manjari SR, Agrawal EK, Keshavan P, Koripella RK, Majumdar S, Marcinkiewicz AL, Lin YP, Agrawal RK, Banavali NK Nat Commun. 2023 Oct 31;14(1):6961. doi: 10.1038/s41467-023-42266-7. PMID:37907464[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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