7uo1: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 7uo1 is ON HOLD
+==E.coli RNaseP Holoenzyme with Mg2+==
+<StructureSection load='7uo1' size='340' side='right'caption='[[7uo1]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7uo1]] is a 3 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=7UO1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UO1 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]] 3.2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=7uo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uo1 OCA], [https://pdbe.org/7uo1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uo1 RCSB], [https://www.ebi.ac.uk/pdbsum/7uo1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uo1 ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Binding of precursor tRNAs (ptRNAs) by bacterial ribonuclease P (RNase P) involves an encounter complex (ES) that isomerizes to a catalytic conformation (ES*). However, the structures of intermediates and the conformational changes that occur during binding are poorly understood. Here, we show that pairing between the 5' leader and 3'RCCA extending the acceptor stem of ptRNA inhibits ES* formation. Cryo-electron microscopy single particle analysis reveals a dynamic enzyme that becomes ordered upon formation of ES* in which extended acceptor stem pairing is unwound. Comparisons of structures with alternative ptRNAs reveals that once unwinding is completed RNase P primarily uses stacking interactions and shape complementarity to accommodate alternative sequences at its cleavage site. Our study reveals active site interactions and conformational changes that drive molecular recognition by RNase P and lays the foundation for understanding how binding interactions are linked to helix unwinding and catalysis.
-Authors: Huang, W., Taylor, D.J.
+Structural and mechanistic basis for recognition of alternative tRNA precursor substrates by bacterial ribonuclease P.,Zhu J, Huang W, Zhao J, Huynh L, Taylor DJ, Harris ME Nat Commun. 2022 Aug 31;13(1):5120. doi: 10.1038/s41467-022-32843-7. PMID:36045135<ref>PMID:36045135</ref>
-Description: E.coli RNaseP Holoenzyme with Mg2+
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Huang, W]]
+<div class="pdbe-citations 7uo1" style="background-color:#fffaf0;"></div>
-[[Category: Taylor, D.J]]
+==See Also==
+*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia coli]]
+[[Category: Large Structures]]
+[[Category: Huang W]]
+[[Category: Taylor DJ]]