1t0k | pdb_00001t0k
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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 supersedes 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 Thu Feb 21 15:08:35 2008
