3E9L
Crystal Structure of Human Prp8, Residues 1755-2016
Summary for 3E9L
| Entry DOI | 10.2210/pdb3e9l/pdb |
| Related | 3E9O 3E9P |
| Descriptor | Pre-mRNA-processing-splicing factor 8, SODIUM ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | nucleotidyl transfer, disease mutation, mrna processing, mrna splicing, nucleus, phosphoprotein, retinitis pigmentosa, rna-binding, sensory transduction, spliceosome, vision, rna binding protein, splicing |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus speckle (By similarity): Q6P2Q9 |
| Total number of polymer chains | 1 |
| Total formula weight | 29593.67 |
| Authors | Pena, V.,Rozov, A.,Wahl, M.C. (deposition date: 2008-08-22, release date: 2008-10-07, Last modification date: 2024-02-21) |
| Primary citation | Pena, V.,Rozov, A.,Fabrizio, P.,Luhrmann, R.,Wahl, M.C. Structure and function of an RNase H domain at the heart of the spliceosome. Embo J., 27:2929-2940, 2008 Cited by PubMed Abstract: Precursor-messenger RNA (pre-mRNA) splicing encompasses two sequential transesterification reactions in distinct active sites of the spliceosome that are transiently established by the interplay of small nuclear (sn) RNAs and spliceosomal proteins. Protein Prp8 is an active site component but the molecular mechanisms, by which it might facilitate splicing catalysis, are unknown. We have determined crystal structures of corresponding portions of yeast and human Prp8 that interact with functional regions of the pre-mRNA, revealing a phylogenetically conserved RNase H fold, augmented by Prp8-specific elements. Comparisons to RNase H-substrate complexes suggested how an RNA encompassing a 5'-splice site (SS) could bind relative to Prp8 residues, which on mutation, suppress splice defects in pre-mRNAs and snRNAs. A truncated RNase H-like active centre lies next to a known contact region of the 5'SS and directed mutagenesis confirmed that this centre is a functional hotspot. These data suggest that Prp8 employs an RNase H domain to help assemble and stabilize the spliceosomal catalytic core, coordinate the activities of other splicing factors and possibly participate in chemical catalysis of splicing. PubMed: 18843295DOI: 10.1038/emboj.2008.209 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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