1xsh
From Proteopedia
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| - | [[Image:1xsh.gif|left|200px]] | + | [[Image:1xsh.gif|left|200px]] |
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| - | '''Solution structure of E.coli RNase P RNA P4 stem oligoribonucleotide, U69C/C70U mutation''' | + | {{Structure |
| + | |PDB= 1xsh |SIZE=350|CAPTION= <scene name='initialview01'>1xsh</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Solution structure of E.coli RNase P RNA P4 stem oligoribonucleotide, U69C/C70U mutation''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1XSH is a [ | + | 1XSH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XSH OCA]. |
==Reference== | ==Reference== | ||
| - | 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:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/15576680 15576680] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Schmitz, M.]] | [[Category: Schmitz, M.]] | ||
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[[Category: u69c/c70u mutant]] | [[Category: u69c/c70u mutant]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:14:04 2008'' |
Revision as of 13:14, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of E.coli RNase P RNA P4 stem oligoribonucleotide, U69C/C70U mutation
Overview
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
1XSH is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
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
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