3BX3
Puf4 T650C/C724R Mutant bound to Cox17 RNA 3' UTR recognition sequence
Summary for 3BX3
Entry DOI | 10.2210/pdb3bx3/pdb |
Related | 1IB2 1M6W 1M8X 1M8Y 1M8Z 3BWT 3BX2 |
Descriptor | COX17 RNA target sequence, Protein PUF4, SULFATE ION (3 entities in total) |
Functional Keywords | puf4, pumilio, rna binding, ho endonuclease, puf4 t650c c724r mutant, transcription, rna binding protein-rna complex, rna binding protein/rna |
Biological source | Saccharomyces cerevisiae (baker's yeast) |
Total number of polymer chains | 4 |
Total formula weight | 81936.95 |
Authors | Miller, M.T.,Higgin, J.J.,Hall, T.M.T. (deposition date: 2008-01-11, release date: 2008-03-11, Last modification date: 2024-02-21) |
Primary citation | Miller, M.T.,Higgin, J.J.,Hall, T.M.T. Basis of altered RNA-binding specificity by PUF proteins revealed by crystal structures of yeast Puf4p Nat.Struct.Mol.Biol., 15:397-402, 2008 Cited by PubMed Abstract: Pumilio/FBF (PUF) family proteins are found in eukaryotic organisms and regulate gene expression post-transcriptionally by binding to sequences in the 3' untranslated region of target transcripts. PUF proteins contain an RNA binding domain that typically comprises eight alpha-helical repeats, each of which recognizes one RNA base. Some PUF proteins, including yeast Puf4p, have altered RNA binding specificity and use their eight repeats to bind to RNA sequences with nine or ten bases. Here we report the crystal structures of Puf4p alone and in complex with a 9-nucleotide (nt) target RNA sequence, revealing that Puf4p accommodates an 'extra' nucleotide by modest adaptations allowing one base to be turned away from the RNA binding surface. Using structural information and sequence comparisons, we created a mutant Puf4p protein that preferentially binds to an 8-nt target RNA sequence over a 9-nt sequence and restores binding of each protein repeat to one RNA base. PubMed: 18327269DOI: 10.1038/nsmb.1390 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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