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2k3r

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Revision as of 10:09, 18 July 2018

Pfu Rpp21 structure and assignments

Structural highlights

2k3r is a 1 chain structure with sequence from Atcc 43587. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	rnp4, PF1613 (ATCC 43587)
Activity:	Ribonuclease P, with EC number 3.1.26.5
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RNP4_PYRFU] Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. The RNA is catalytic, but its KM for pre-tRNA is 170-fold decreased in the presence of the 4 known protein subunits (Rnp1-4). The protein subunits also decrease the amount of Mg(2+) needed for activity.^[1] ^[2] ^[3]

Publication Abstract from PubMed

RNase P is the ubiquitous ribonucleoprotein metalloenzyme responsible for cleaving the 5'-leader sequence of precursor tRNAs during their maturation. While the RNA subunit is catalytically active on its own at high monovalent and divalent ion concentrations, four protein subunits are associated with archaeal RNase P activity in vivo: RPP21, RPP29, RPP30, and POP5. These proteins have been shown to function in pairs: RPP21-RPP29 and POP5-RPP30. We have determined the solution structure of RPP21 from the hyperthermophilic archaeon Pyrococcus furiosus ( Pfu) using conventional and paramagnetic NMR techniques. Pfu RPP21 in solution consists of an unstructured N-terminus, two alpha-helices, a zinc binding motif, and an unstructured C-terminus. Moreover, we have used chemical shift perturbations to characterize the interaction of RPP21 with RPP29. The data show that the primary contact with RPP29 is localized to the two helices of RPP21. This information represents a fundamental step toward understanding structure-function relationships of the archaeal RNase P holoenzyme.

Solution structure of Pyrococcus furiosus RPP21, a component of the archaeal RNase P holoenzyme, and interactions with its RPP29 protein partner.,Amero CD, Boomershine WP, Xu Y, Foster M Biochemistry. 2008 Nov 11;47(45):11704-10. Epub 2008 Oct 16. PMID:18922021^[4]

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

References

↑ Tsai HY, Pulukkunat DK, Woznick WK, Gopalan V. Functional reconstitution and characterization of Pyrococcus furiosus RNase P. Proc Natl Acad Sci U S A. 2006 Oct 31;103(44):16147-52. Epub 2006 Oct 19. PMID:17053064 doi:http://dx.doi.org/10.1073/pnas.0608000103
↑ Chen WY, Xu Y, Cho IM, Oruganti SV, Foster MP, Gopalan V. Cooperative RNP assembly: complementary rescue of structural defects by protein and RNA subunits of archaeal RNase P. J Mol Biol. 2011 Aug 12;411(2):368-83. doi: 10.1016/j.jmb.2011.05.012. Epub 2011 , Jun 12. PMID:21683084 doi:http://dx.doi.org/10.1016/j.jmb.2011.05.012
↑ Chen WY, Singh D, Lai LB, Stiffler MA, Lai HD, Foster MP, Gopalan V. Fidelity of tRNA 5'-maturation: a possible basis for the functional dependence of archaeal and eukaryal RNase P on multiple protein cofactors. Nucleic Acids Res. 2012 May;40(10):4666-80. doi: 10.1093/nar/gks013. Epub 2012, Jan 31. PMID:22298511 doi:http://dx.doi.org/10.1093/nar/gks013
↑ Amero CD, Boomershine WP, Xu Y, Foster M. Solution structure of Pyrococcus furiosus RPP21, a component of the archaeal RNase P holoenzyme, and interactions with its RPP29 protein partner. Biochemistry. 2008 Nov 11;47(45):11704-10. Epub 2008 Oct 16. PMID:18922021 doi:10.1021/bi8015982

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2k3r"

@@ Line 1: / Line 1: @@
 ==Pfu Rpp21 structure and assignments==
 <StructureSection load='2k3r' size='340' side='right' caption='[[2k3r]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rnp4, PF1613 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 ATCC 43587])</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=2k3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k3r OCA], [http://pdbe.org/2k3r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k3r RCSB], [http://www.ebi.ac.uk/pdbsum/2k3r PDBsum]</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=2k3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k3r OCA], [http://pdbe.org/2k3r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k3r RCSB], [http://www.ebi.ac.uk/pdbsum/2k3r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2k3r ProSAT]</span></td></tr>
 </table>
 == Function ==

2k3r

From Proteopedia

Revision as of 10:09, 18 July 2018

Pfu Rpp21 structure and assignments

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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