9h3v

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Current revision (10:23, 22 January 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9h3v is ON HOLD until Paper Publication
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==50S subunit precursor C-CP_L2-L28==
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<StructureSection load='9h3v' size='340' side='right'caption='[[9h3v]], [[Resolution|resolution]] 3.55&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9h3v]] 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=9H3V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9H3V FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.55&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9h3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9h3v OCA], [https://pdbe.org/9h3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9h3v RCSB], [https://www.ebi.ac.uk/pdbsum/9h3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9h3v ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RL2_ECOLI RL2_ECOLI] One of the primary rRNA binding proteins. Located near the base of the L1 stalk, it is probably also mobile. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is highly controversial.[HAMAP-Rule:MF_01320_B] In the E.coli 70S ribosome in the initiation state it has been modeled to make several contacts with the 16S rRNA (forming bridge B7b, PubMed:12809609); these contacts are broken in the model with bound EF-G.[HAMAP-Rule:MF_01320_B]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The proline-rich antimicrobial designer peptide Api137 inhibits protein expression in bacteria by binding simultaneously to the ribosomal polypeptide exit tunnel and the release factor (RF), depleting the cellular RF pool and leading to ribosomal arrest at stop codons. This study investigates the additional effect of Api137 on the assembly of ribosomes using an Escherichia coli reporter strain expressing one ribosomal protein per 30S and 50S subunit tagged with mCherry and EGFP, respectively. Separation of cellular extracts derived from cells exposed to Api137 in a sucrose gradient reveals elevated levels of partially assembled and not fully matured precursors of the 50S subunit (pre-50S). High-resolution structures obtained by cryogenic electron microscopy demonstrate that a large proportion of pre-50S states are missing up to five proteins (uL22, bL32, uL29, bL23, and uL16) and have misfolded helices in 23S rRNA domain IV. These data suggest a second mechanism for Api137, wherein it disrupts 50S subunit assembly by inducing the formation of misfolded precursor particles potentially incapable of evolving into active ribosomes, suggesting a bactericidal mechanism.
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Authors:
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The proline-rich antimicrobial peptide Api137 disrupts large ribosomal subunit assembly and induces misfolding.,Lauer SM, Gasse J, Krizsan A, Reepmeyer M, Sprink T, Nikolay R, Spahn CMT, Hoffmann R Nat Commun. 2025 Jan 10;16(1):567. doi: 10.1038/s41467-025-55836-8. PMID:39794318<ref>PMID:39794318</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 9h3v" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Lauer S]]
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[[Category: Nikolay R]]
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[[Category: Spahn CMT]]

Current revision

50S subunit precursor C-CP_L2-L28

PDB ID 9h3v

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