2l9w | pdb_00002l9w

Solution Structure of the C-terminal domain of Prp24

spinqualitylabelsall models 2l9w Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2l9w is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PRP24_YEAST Binds preferentially to the U4/U6 hybrid snRNAs. Can stimulate the annealing of U4 and U6. Could participate in both the formation and disassembly of the U4/U6 hybrid during splicing. Publication Abstract from PubMed The essential splicing factor Prp24 contains four RNA Recognition Motif (RRM) domains, and functions to anneal U6 and U4 RNAs during spliceosome assembly. Here, we report the structure and characterization of the C-terminal RRM4. This domain adopts a novel non-canonical RRM fold with two additional flanking alpha-helices that occlude its beta-sheet face, forming an occluded RRM (oRRM) domain. The flanking helices form a large electropositive surface. oRRM4 binds to and unwinds the U6 internal stem loop (U6 ISL), a stable helix that must be unwound during U4/U6 assembly. NMR data indicate that the process starts with the terminal base pairs of the helix and proceeds toward the loop. We propose a mechanistic and structural model of Prp24's annealing activity in which oRRM4 functions to destabilize the U6 ISL during U4/U6 assembly. A novel occluded RNA recognition motif in Prp24 unwinds the U6 RNA internal stem loop.,Martin-Tumasz S, Richie AC, Clos LJ 2nd, Brow DA, Butcher SE Nucleic Acids Res. 2011 Jun 7. PMID:21653550 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pre-mRNA splicing factors 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA