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[[Image:3q1r.png|left|200px]]
==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=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3q1r]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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>
<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='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 Thermotoga maritima])</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://www.rcsb.org/pdb/explore.do?structureId=3q1r RCSB], [http://www.ebi.ac.uk/pdbsum/3q1r PDBsum]</span></td></tr>
</table>
<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_3q1r|  PDB=3q1r  |  SCENE=  }}
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>


===Crystal structure of a bacterial RNase P holoenzyme in complex with TRNA and in the presence of 5' leader===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_21076397}}
 
==About this Structure==
[[3q1r]] is a 4 chain structure with sequence from [http://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].


==See Also==
==See Also==
*[[Ribonuclease|Ribonuclease]]
*[[Ribonuclease|Ribonuclease]]
 
*[[User:Jaime.Prilusky/Test/tree|User:Jaime.Prilusky/Test/tree]]
==Reference==
== References ==
<ref group="xtra">PMID:021076397</ref><references group="xtra"/>
<references/>
__TOC__
</StructureSection>
[[Category: Ribonuclease P]]
[[Category: Ribonuclease P]]
[[Category: Thermotoga maritima]]
[[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, N J]]
[[Category: Swinger, K K.]]
[[Category: Swinger, K K]]
[[Category: Torres-Larios, A.]]
[[Category: Torres-Larios, A]]
[[Category: A-minor interaction]]
[[Category: A-minor interaction]]
[[Category: Base stacking]]
[[Category: Base stacking]]

Revision as of 16:31, 9 December 2014

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.
Ligands:
Gene:rnpA, RNPA OR TM1463, RNPB, TM_1463 (Thermotoga maritima)
Activity:Ribonuclease P, with EC number 3.1.26.5
Resources:FirstGlance, OCA, RCSB, PDBsum

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[1]

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

See Also

References

  1. ↑ Reiter NJ, Osterman A, Torres-Larios A, Swinger KK, Pan T, Mondragon A. Structure of a bacterial ribonuclease P holoenzyme in complex with tRNA. Nature. 2010 Nov 14. PMID:21076397 doi:10.1038/nature09516

3q1r, resolution 4.21Å

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