1xsu: Difference between revisions

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New page: left|200px<br /><applet load="1xsu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xsu" /> '''Solution structure of E.coli RNase P RNA P4 ...
 
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[[Image:1xsu.gif|left|200px]]<br /><applet load="1xsu" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Solution structure of E.coli RNase P RNA P4 stem, U69C/C70U mutation, complexed with cobalt (III) hexammine.'''<br />


==Overview==
==Solution structure of E.coli RNase P RNA P4 stem, U69C/C70U mutation, complexed with cobalt (III) hexammine.==
The solution structures of two 27 nt RNA hairpins and their complexes with, cobalt(III)-hexammine [Co(NH(3))(6)(3+)] were determined by NMR, spectroscopy. The RNA hairpins are variants of the P4 region from, Escherichia coli RNase P RNA: a U-to-A mutant changing the identity of the, bulged nucleotide, and a U-to-C, C-to-U double mutant changing only the, bulge position. Structures calculated from NMR constraints show that the, RNA hairpins adopt different conformations. In the U-to-C, C-to-U double, mutant, the conserved bulged uridine in the P4 wild-type stem is found to, be shifted in the 3'-direction by one nucleotide when compared with the, wild-type structure. Co(NH(3))(6)(3+) is used as a spectroscopic probe for, Mg(H(2)O)(6)(2+) binding sites because both complexes have octahedral, symmetry and have similar radii. Intermolecular NOE crosspeaks between, Co(NH(3))(6)(3+) and RNA protons were used to locate the site of, Co(NH(3))(6)(3+) binding to both RNA hairpins. The metal ion binds in the, major groove near a bulge loop in both mutants, but is shifted 3' by about, one base pair in the double mutant. The change of the metal ion binding, site is compared with results obtained on corresponding mutant RNase P RNA, molecules as reported by Harris and co-workers (RNA, 1, 210-218).
<StructureSection load='1xsu' size='340' side='right'caption='[[1xsu]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1xsu]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XSU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XSU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NCO:COBALT+HEXAMMINE(III)'>NCO</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=1xsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xsu OCA], [https://pdbe.org/1xsu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xsu RCSB], [https://www.ebi.ac.uk/pdbsum/1xsu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xsu ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The solution structures of two 27 nt RNA hairpins and their complexes with cobalt(III)-hexammine [Co(NH(3))(6)(3+)] were determined by NMR spectroscopy. The RNA hairpins are variants of the P4 region from Escherichia coli RNase P RNA: a U-to-A mutant changing the identity of the bulged nucleotide, and a U-to-C, C-to-U double mutant changing only the bulge position. Structures calculated from NMR constraints show that the RNA hairpins adopt different conformations. In the U-to-C, C-to-U double mutant, the conserved bulged uridine in the P4 wild-type stem is found to be shifted in the 3'-direction by one nucleotide when compared with the wild-type structure. Co(NH(3))(6)(3+) is used as a spectroscopic probe for Mg(H(2)O)(6)(2+) binding sites because both complexes have octahedral symmetry and have similar radii. Intermolecular NOE crosspeaks between Co(NH(3))(6)(3+) and RNA protons were used to locate the site of Co(NH(3))(6)(3+) binding to both RNA hairpins. The metal ion binds in the major groove near a bulge loop in both mutants, but is shifted 3' by about one base pair in the double mutant. The change of the metal ion binding site is compared with results obtained on corresponding mutant RNase P RNA molecules as reported by Harris and co-workers (RNA, 1, 210-218).


==About this Structure==
Change of RNase P RNA function by single base mutation correlates with perturbation of metal ion binding in P4 as determined by NMR spectroscopy.,Schmitz M Nucleic Acids Res. 2004 Dec 2;32(21):6358-66. Print 2004. PMID:15576680<ref>PMID:15576680</ref>
1XSU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with NCO as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XSU OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Change of RNase P RNA function by single base mutation correlates with perturbation of metal ion binding in P4 as determined by NMR spectroscopy., Schmitz M, Nucleic Acids Res. 2004 Dec 2;32(21):6358-66. Print 2004. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15576680 15576680]
</div>
[[Category: Protein complex]]
<div class="pdbe-citations 1xsu" style="background-color:#fffaf0;"></div>
[[Category: Schmitz, M.]]
[[Category: NCO]]
[[Category: cobalt (iii) hexammine complex]]
[[Category: metal binding site]]
[[Category: metal complex]]
[[Category: p4 stem]]
[[Category: ribonuclease p rna]]
[[Category: ribozyme]]
[[Category: transfer rna processing]]
[[Category: u69c/c70u mutant]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:50:54 2007''
==See Also==
*[[Ribozyme 3D structures|Ribozyme 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Schmitz M]]

Latest revision as of 12:29, 6 December 2023

Solution structure of E.coli RNase P RNA P4 stem, U69C/C70U mutation, complexed with cobalt (III) hexammine.Solution structure of E.coli RNase P RNA P4 stem, U69C/C70U mutation, complexed with cobalt (III) hexammine.

Structural highlights

1xsu is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

The solution structures of two 27 nt RNA hairpins and their complexes with cobalt(III)-hexammine [Co(NH(3))(6)(3+)] were determined by NMR spectroscopy. The RNA hairpins are variants of the P4 region from Escherichia coli RNase P RNA: a U-to-A mutant changing the identity of the bulged nucleotide, and a U-to-C, C-to-U double mutant changing only the bulge position. Structures calculated from NMR constraints show that the RNA hairpins adopt different conformations. In the U-to-C, C-to-U double mutant, the conserved bulged uridine in the P4 wild-type stem is found to be shifted in the 3'-direction by one nucleotide when compared with the wild-type structure. Co(NH(3))(6)(3+) is used as a spectroscopic probe for Mg(H(2)O)(6)(2+) binding sites because both complexes have octahedral symmetry and have similar radii. Intermolecular NOE crosspeaks between Co(NH(3))(6)(3+) and RNA protons were used to locate the site of Co(NH(3))(6)(3+) binding to both RNA hairpins. The metal ion binds in the major groove near a bulge loop in both mutants, but is shifted 3' by about one base pair in the double mutant. The change of the metal ion binding site is compared with results obtained on corresponding mutant RNase P RNA molecules as reported by Harris and co-workers (RNA, 1, 210-218).

Change of RNase P RNA function by single base mutation correlates with perturbation of metal ion binding in P4 as determined by NMR spectroscopy.,Schmitz M Nucleic Acids Res. 2004 Dec 2;32(21):6358-66. Print 2004. PMID:15576680[1]

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

See Also

References

  1. Schmitz M. Change of RNase P RNA function by single base mutation correlates with perturbation of metal ion binding in P4 as determined by NMR spectroscopy. Nucleic Acids Res. 2004 Dec 2;32(21):6358-66. Print 2004. PMID:15576680 doi:32/21/6358
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