7og5: Difference between revisions

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==RNA-free Ribonuclease P from Halorhodospira halophila==

== Structural highlights ==

<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OG5 FirstGlance]. <br>

</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=7og5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7og5 OCA], [https://pdbe.org/7og5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7og5 RCSB], [https://www.ebi.ac.uk/pdbsum/7og5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7og5 ProSAT]</span></td></tr>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.37Å</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=7og5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7og5 OCA], [https://pdbe.org/7og5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7og5 RCSB], [https://www.ebi.ac.uk/pdbsum/7og5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7og5 ProSAT]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

Endonucleolytic removal of 5'-leader sequences from tRNA precursor transcripts (pre-tRNAs) by RNase P is essential for protein synthesis. Beyond RNA-based RNase P enzymes, protein-only versions of the enzyme exert this function in various Eukarya (there termed PRORPs) and in some bacteria (Aquifex aeolicus and close relatives); both enzyme types belong to distinct subgroups of the PIN domain metallonuclease superfamily. Homologs of Aquifex RNase P (HARPs) are also expressed in some other bacteria and many archaea, where they coexist with RNA-based RNase P and do not represent the main RNase P activity. Here we solved the structure of the bacterial HARP from Halorhodospira halophila by cryo-EM revealing a novel screw-like dodecameric assembly. Biochemical experiments demonstrate that oligomerization is required for RNase P activity of HARPs. We propose that the tRNA substrate binds to an extended spike-helix (SH) domain that protrudes from the screw-like assembly to position the 5'-end in close proximity to the active site of the neighboring dimer. The structure suggests that eukaryotic PRORPs and prokaryotic HARPs recognize the same structural elements of pre-tRNAs (tRNA elbow region and cleavage site). Our analysis thus delivers the structural and mechanistic basis for pre-tRNA processing by the prokaryotic HARP system.

Structure and mechanistic features of the prokaryotic minimal RNase P.,Feyh R, Waeber NB, Prinz S, Giammarinaro PI, Bange G, Hochberg G, Hartmann RK, Altegoer F Elife. 2021 Jun 28;10. pii: 70160. doi: 10.7554/eLife.70160. PMID:34180399<ref>PMID:34180399</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

==See Also==

*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]

== References ==

__TOC__

</StructureSection>

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 ==RNA-free Ribonuclease P from Halorhodospira halophila==
-<StructureSection load='7og5' size='340' side='right'caption='[[7og5]]' scene=''>
+<StructureSection load='7og5' size='340' side='right'caption='[[7og5]], [[Resolution|resolution]] 3.37&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OG5 FirstGlance]. <br>
-</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=7og5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7og5 OCA], [https://pdbe.org/7og5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7og5 RCSB], [https://www.ebi.ac.uk/pdbsum/7og5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7og5 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.37&#8491;</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=7og5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7og5 OCA], [https://pdbe.org/7og5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7og5 RCSB], [https://www.ebi.ac.uk/pdbsum/7og5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7og5 ProSAT]</span></td></tr>
 </table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Endonucleolytic removal of 5'-leader sequences from tRNA precursor transcripts (pre-tRNAs) by RNase P is essential for protein synthesis. Beyond RNA-based RNase P enzymes, protein-only versions of the enzyme exert this function in various Eukarya (there termed PRORPs) and in some bacteria (Aquifex aeolicus and close relatives); both enzyme types belong to distinct subgroups of the PIN domain metallonuclease superfamily. Homologs of Aquifex RNase P (HARPs) are also expressed in some other bacteria and many archaea, where they coexist with RNA-based RNase P and do not represent the main RNase P activity. Here we solved the structure of the bacterial HARP from Halorhodospira halophila by cryo-EM revealing a novel screw-like dodecameric assembly. Biochemical experiments demonstrate that oligomerization is required for RNase P activity of HARPs. We propose that the tRNA substrate binds to an extended spike-helix (SH) domain that protrudes from the screw-like assembly to position the 5'-end in close proximity to the active site of the neighboring dimer. The structure suggests that eukaryotic PRORPs and prokaryotic HARPs recognize the same structural elements of pre-tRNAs (tRNA elbow region and cleavage site). Our analysis thus delivers the structural and mechanistic basis for pre-tRNA processing by the prokaryotic HARP system.
+Structure and mechanistic features of the prokaryotic minimal RNase P.,Feyh R, Waeber NB, Prinz S, Giammarinaro PI, Bange G, Hochberg G, Hartmann RK, Altegoer F Elife. 2021 Jun 28;10. pii: 70160. doi: 10.7554/eLife.70160. PMID:34180399<ref>PMID:34180399</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 7og5" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>