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==Crystal structure of a bacterial RNase P holoenzyme in complex with TRNA and in the presence of 5' leader==
==Crystal structure of a bacterial RNase P holoenzyme in complex with TRNA and in the presence of 5' leader==
<StructureSection load='3q1r' size='340' side='right' caption='[[3q1r]], [[Resolution|resolution]] 4.21&Aring;' scene=''>
<StructureSection load='3q1r' size='340' side='right'caption='[[3q1r]], [[Resolution|resolution]] 4.21&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3q1r]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3okb 3okb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q1R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q1R FirstGlance]. <br>
<table><tr><td colspan='2'>[[3q1r]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3okb 3okb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q1R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q1R FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.21&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2a2e|2a2e]], [[2a64|2a64]], [[1u9s|1u9s]], [[1nbs|1nbs]], [[1nz0|1nz0]], [[1ehz|1ehz]], [[3q1q|3q1q]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rnpA, RNPA OR TM1463, RNPB, TM_1463 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</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=3q1r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q1r OCA], [https://pdbe.org/3q1r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q1r RCSB], [https://www.ebi.ac.uk/pdbsum/3q1r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q1r ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonuclease_P Ribonuclease P], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.5 3.1.26.5] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3q1r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q1r OCA], [http://pdbe.org/3q1r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3q1r RCSB], [http://www.ebi.ac.uk/pdbsum/3q1r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3q1r ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/RNPA_THEMA RNPA_THEMA]] 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 (By similarity).  
[https://www.uniprot.org/uniprot/RNPA_THEMA RNPA_THEMA] 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 (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ribonuclease (RNase) P is the universal ribozyme responsible for 5'-end tRNA processing. We report the crystal structure of the Thermotoga maritima RNase P holoenzyme in complex with tRNA(Phe). The 154 kDa complex consists of a large catalytic RNA (P RNA), a small protein cofactor and a mature tRNA. The structure shows that RNA-RNA recognition occurs through shape complementarity, specific intermolecular contacts and base-pairing interactions. Soaks with a pre-tRNA 5' leader sequence with and without metal help to identify the 5' substrate path and potential catalytic metal ions. The protein binds on top of a universally conserved structural module in P RNA and interacts with the leader, but not with the mature tRNA. The active site is composed of phosphate backbone moieties, a universally conserved uridine nucleobase, and at least two catalytically important metal ions. The active site structure and conserved RNase P-tRNA contacts suggest a universal mechanism of catalysis by RNase P.
 
Structure of a bacterial ribonuclease P holoenzyme in complex with tRNA.,Reiter NJ, Osterman A, Torres-Larios A, Swinger KK, Pan T, Mondragon A Nature. 2010 Nov 14. PMID:21076397<ref>PMID:21076397</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3q1r" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Ribonuclease|Ribonuclease]]
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
*[[TRNA|TRNA]]
*[[Transfer RNA (tRNA)|Transfer RNA (tRNA)]]
*[[Temp|Temp]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 43589]]
[[Category: Large Structures]]
[[Category: Ribonuclease P]]
[[Category: Thermotoga maritima]]
[[Category: Mondragon, A]]
[[Category: Mondragon A]]
[[Category: Ostermanm, A]]
[[Category: Ostermanm A]]
[[Category: Pan, T]]
[[Category: Pan T]]
[[Category: Reiter, N J]]
[[Category: Reiter NJ]]
[[Category: Swinger, K K]]
[[Category: Swinger KK]]
[[Category: Torres-Larios, A]]
[[Category: Torres-Larios A]]
[[Category: A-minor interaction]]
[[Category: Base stacking]]
[[Category: Endonuclease]]
[[Category: Enzyme-product complex]]
[[Category: Hydrolase-rna complex]]
[[Category: Intermolecular base pair]]
[[Category: Intermolecular rna-rna contact]]
[[Category: Metalloenzyme]]
[[Category: Pre-trna]]
[[Category: Ribonuclease p]]
[[Category: Ribonucleoprotein complex]]
[[Category: Ribose zipper]]
[[Category: Ribozyme]]
[[Category: Rna-metal interaction]]
[[Category: Rnase p]]
[[Category: Rnp]]
[[Category: Shape complementarity]]
[[Category: Substrate recognition]]
[[Category: Tetraloop-receptor]]
[[Category: Trna]]

Latest revision as of 14:30, 14 March 2024

Crystal structure of a bacterial RNase P holoenzyme in complex with TRNA and in the presence of 5' leaderCrystal structure of a bacterial RNase P holoenzyme in complex with TRNA and in the presence of 5' leader

Structural highlights

3q1r is a 4 chain structure with sequence from Thermotoga maritima. This structure supersedes the now removed PDB entry 3okb. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 4.21Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RNPA_THEMA 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 (By similarity).

See Also

3q1r, resolution 4.21Å

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