1T0K

Joint X-ray and NMR Refinement of Yeast L30e-mRNA complex

Replaces:  1CK5Replaces:  1CK8Replaces:  1CN8Replaces:  1CN9

Summary for 1T0K

• Entry DOI: 10.2210/pdb1t0k/pdb
• Related PRD ID: PRD_900010
• Descriptor: 5'-R(*GP*AP*CP*CP*GP*GP*AP*GP*UP*GP*UP*CP*C)-3', 5'-R(*G*GP*AP*CP*GP*CP*AP*GP*AP*GP*AP*UP*GP*GP*UP*C)-3', Maltose-binding periplasmic protein, ... (5 entities in total)
• Functional Keywords: joint nmr and x-ray refinement, ribosomal protein l30e, mbp fusion protein, ribosome
• Biological source: Escherichia coli; More
• Cellular location: Periplasm: P02928; Cytoplasm (By similarity): P14120
• Total number of polymer chains: 4
• Total formula weight: 63255.85

Authors

Chao, J.A.,Williamson, J.R. (deposition date: 2004-04-09, release date: 2004-07-20, Last modification date: 2024-05-22)

Primary citation

Chao, J.A.,Williamson, J.R.
Joint X-Ray and NMR Refinement of the Yeast L30e-mRNA Complex
Structure, 12:1165-1176, 2004

PubMed Abstract: 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.

PubMed: 15242593
DOI: 10.1016/j.str.2004.04.023

Experimental method

X-RAY DIFFRACTION (3.24 Å)