2I91

60kDa Ro autoantigen in complex with a fragment of misfolded RNA

Summary for 2I91

• Entry DOI: 10.2210/pdb2i91/pdb
• Descriptor: 5'-R(*GP*CP*CP*UP*AP*CP*CP*C)-3', 5'-R(*C*GP*GP*UP*AP*GP*GP*CP*UP*UP*UP*UP*CP*AP*A)-3', 60 kDa SS-A/Ro ribonucleoprotein, ... (6 entities in total)
• Functional Keywords: von willebrand factor a, rossmann-fold, heat repeat, midas motif, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Xenopus laevis (African clawed frog)
• Cellular location: Cytoplasm: P42700
• Total number of polymer chains: 6
• Total formula weight: 136174.24

Authors

Reinisch, K.M.,Stein, A.J. (deposition date: 2006-09-04, release date: 2006-10-17, Last modification date: 2023-08-30)

Primary citation

Fuchs, G.,Stein, A.J.,Fu, C.,Reinisch, K.M.,Wolin, S.L.
Structural and biochemical basis for misfolded RNA recognition by the Ro autoantigen.
Nat.Struct.Mol.Biol., 13:1002-1009, 2006

PubMed Abstract: The Ro autoantigen is ring-shaped, binds misfolded noncoding RNAs and is proposed to function in quality control. Here we determine how Ro interacts with misfolded RNAs. Binding of Ro to misfolded precursor (pre)-5S ribosomal RNA requires a single-stranded 3' end and helical elements. As mutating most sequences of the helices and tail results in modest decreases in binding, Ro may be able to associate with a range of RNAs. Ro binds several other RNAs that contain single-stranded tails. A crystal structure of Ro bound to a misfolded pre-5S rRNA fragment reveals that the tail inserts into the cavity, while a helix binds on the surface. Most contacts of Ro with the helix are to the backbone. Mutagenesis reveals that Ro has an extensive RNA-binding surface. We propose that Ro uses this surface to scavenge RNAs that fail to bind their specific RNA-binding proteins.

PubMed: 17041599
DOI: 10.1038/nsmb1156

Experimental method

X-RAY DIFFRACTION (2.65 Å)