1CK2

YEAST (SACCHAROMYCES CEREVISIAE) RIBOSOMAL PROTEIN L30

Summary for 1CK2

• Entry DOI: 10.2210/pdb1ck2/pdb
• Descriptor: 60S RIBOSOMAL PROTEIN L30 (1 entity in total)
• Functional Keywords: ribosomal protein, auto-regulation of pre-mrna splicing and mrna translation, ribosome
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 11299.17

Authors

Mao, H.,Willamson, J.R. (deposition date: 1999-04-26, release date: 1999-10-14, Last modification date: 2023-12-27)

Primary citation

Mao, H.,Williamson, J.R.
Local folding coupled to RNA binding in the yeast ribosomal protein L30
J.Mol.Biol., 292:345-359, 1999

PubMed Abstract: The ribosomal protein L30 from yeast Saccharomyces cerevisiae auto-regulates its own synthesis by binding to a structural element in both its pre-mRNA and its mRNA. The three-dimensional structures of L30 in the free (f L30) and the pre-mRNA bound (b L30) forms have been solved by nuclear magnetic resonance spectroscopy. Both protein structures contain four alternating alpha-helices and four beta-strands segments and adopt an overall topology that is an alphabetaalpha three-layer sandwich, representing a unique fold. Three loops on one end of the alphabetaalpha sandwich have been mapped as the RNA binding site on the basis of structural comparison, chemical shift perturbation and the inter-molecular nuclear Overhauser effects to the RNA. The structural and dynamic comparison of f L30 and b L30 reveals that local dynamics may play an important role in the RNA binding. The fourth helix in b L30 is longer than in f L30, and is stabilized by RNA binding. The exposed hydrophobic surface that is buried upon RNA binding may provide the energy necessary to drive secondary structure formation, and may account for the increased stability of b L30.

PubMed: 10493880
DOI: 10.1006/jmbi.1999.3044

Experimental method

SOLUTION NMR