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1t0k
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(New page: 200px<br /><applet load="1t0k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t0k, resolution 3.24Å" /> '''Joint X-ray and NMR ...)
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Revision as of 00:46, 21 November 2007
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Joint X-ray and NMR Refinement of Yeast L30e-mRNA complex
Overview
L30e, a Saccharomyces cervisiae ribosomal protein, regulates its own, expression by binding to a purine-rich asymmetric internal loop located in, both its pre-mRNA and mature mRNA. A crystal structure of an MBP-L30e, fusion protein in complex with an RNA containing the pre-mRNA regulatory, site was solved at 3.24 A. Interestingly, the structure of the RNA, differed from that observed in a previously determined NMR structure of, the complex. Analysis of the NMR data led to the identification of a, single imino proton resonance in the internal loop that had been, incorrectly assigned and was principally responsible for the erroneous RNA, structure. A structure refinement was performed using both the X-ray, diffraction data and the NMR-derived distance and angle restraints. The, joint NMR and X-ray refinement resulted in improved stereochemistry and, lower crystallographic R factors. The RNA internal loop of the, MBP-L30e-mRNA complex adopts the canonical K-turn fold.
About this Structure
1T0K is a Protein complex structure of sequences from Escherichia coli and Saccharomyces cerevisiae with MTT as ligand. This structure superseeds the now removed PDB entries 1CK5, 1CK8, 1CN8 and 1CN9. Full crystallographic information is available from OCA.
Reference
Joint X-ray and NMR refinement of the yeast L30e-mRNA complex., Chao JA, Williamson JR, Structure. 2004 Jul;12(7):1165-76. PMID:15242593
Page seeded by OCA on Wed Nov 21 02:53:51 2007
