7uo2: Difference between revisions
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==E.coli RNaseP Holoenzyme with Mg2+== | |||
<StructureSection load='7uo2' size='340' side='right'caption='[[7uo2]], [[Resolution|resolution]] 3.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7uo2]] is a 2 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=7UO2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UO2 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7uo2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uo2 OCA], [https://pdbe.org/7uo2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uo2 RCSB], [https://www.ebi.ac.uk/pdbsum/7uo2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uo2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[https://www.uniprot.org/uniprot/C3SLK7_ECOLX C3SLK7_ECOLX]] RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.[ARBA:ARBA00002663][HAMAP-Rule:MF_00227] | |||
<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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7uo2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | |||
[[Category: Huang W]] | |||
[[Category: Taylor DJ]] | |||
Revision as of 09:16, 28 September 2022
E.coli RNaseP Holoenzyme with Mg2+E.coli RNaseP Holoenzyme with Mg2+
Structural highlights
Function[C3SLK7_ECOLX] RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.[ARBA:ARBA00002663][HAMAP-Rule:MF_00227] Publication Abstract from PubMedBinding 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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