3K5Z

Crystal structure of FBF-2/gld-1 FBEa G4A mutant complex

Summary for 3K5Z

• Entry DOI: 10.2210/pdb3k5z/pdb
• Related: 3K5Q 3K5Y 3K61 3K62 3K64
• Descriptor: Fem-3 mRNA-binding factor 2, 5'-R(*UP*GP*UP*AP*CP*CP*AP*UP*A)-3' (3 entities in total)
• Functional Keywords: fbf, fem-3 binding factor, puf, rna-binding specificity, base flipping, base stacking, rna-rna binding protein complex, rna/rna binding protein
• Biological source: Caenorhabditis elegans (nematode)
• Cellular location: Cytoplasm (By similarity): Q09312
• Total number of polymer chains: 2
• Total formula weight: 49778.73

Authors

Wang, Y.,Opperman, L.,Wickens, M.,Hall, T.M.T. (deposition date: 2009-10-08, release date: 2009-11-03, Last modification date: 2023-09-06)

Primary citation

Wang, Y.,Opperman, L.,Wickens, M.,Hall, T.M.
Structural basis for specific recognition of multiple mRNA targets by a PUF regulatory protein.
Proc.Natl.Acad.Sci.USA, 106:20186-20191, 2009

PubMed Abstract: Caenorhabditis elegans fem-3 binding factor (FBF) is a founding member of the PUMILIO/FBF (PUF) family of mRNA regulatory proteins. It regulates multiple mRNAs critical for stem cell maintenance and germline development. Here, we report crystal structures of FBF in complex with 6 different 9-nt RNA sequences, including elements from 4 natural mRNAs. These structures reveal that FBF binds to conserved bases at positions 1-3 and 7-8. The key specificity determinant of FBF vs. other PUF proteins lies in positions 4-6. In FBF/RNA complexes, these bases stack directly with one another and turn away from the RNA-binding surface. A short region of FBF is sufficient to impart its unique specificity and lies directly opposite the flipped bases. We suggest that this region imposes a flattened curvature on the protein; hence, the requirement for the additional nucleotide. The principles of FBF/RNA recognition suggest a general mechanism by which PUF proteins recognize distinct families of RNAs yet exploit very nearly identical atomic contacts in doing so.

PubMed: 19901328
DOI: 10.1073/pnas.0812076106

Experimental method

X-RAY DIFFRACTION (2.4 Å)