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2GO9

RRM domains 1 and 2 of Prp24 from S. cerevisiae

Summary for 2GO9
Entry DOI10.2210/pdb2go9/pdb
NMR InformationBMRB: 7070
DescriptorU4/U6 snRNA-associated splicing factor PRP24 (1 entity in total)
Functional Keywordsbeta-alpha-beta, rrm, rbd, rna binding protein
Biological sourceSaccharomyces cerevisiae (baker's yeast)
Cellular locationNucleus: P49960
Total number of polymer chains1
Total formula weight18626.58
Authors
Reiter, N.J.,Lee, D.H.,Tonelli, M.,Kwan, S.K.,Brow, D.A.,Butcher, S.E. (deposition date: 2006-04-12, release date: 2007-02-27, Last modification date: 2024-05-29)
Primary citationBae, E.,Reiter, N.J.,Bingman, C.A.,Kwan, S.S.,Lee, D.,Phillips, G.N.,Butcher, S.E.,Brow, D.A.
Structure and interactions of the first three RNA recognition motifs of splicing factor prp24.
J.Mol.Biol., 367:1447-1458, 2007
Cited by
PubMed Abstract: The essential Saccharomyces cerevisiae pre-messenger RNA splicing protein 24 (Prp24) has four RNA recognition motifs (RRMs) and facilitates U6 RNA base-pairing with U4 RNA during spliceosome assembly. Prp24 is a component of the free U6 small nuclear ribonucleoprotein particle (snRNP) but not the U4/U6 bi-snRNP, and so is thought to be displaced from U6 by U4/U6 base-pairing. The interaction partners of each of the four RRMs of Prp24 and how these interactions direct U4/U6 pairing are not known. Here we report the crystal structure of the first three RRMs and the solution structure of the first two RRMs of Prp24. Strikingly, RRM 2 forms extensive inter-domain contacts with RRMs 1 and 3. These contacts occupy much of the canonical RNA-binding faces (beta-sheets) of RRMs 1 and 2, but leave the beta-sheet of RRM 3 exposed. Previously identified substitutions in Prp24 that suppress mutations in U4 and U6 spliceosomal RNAs cluster primarily in the beta-sheet of RRM 3, but also in a conserved loop of RRM 2. RNA binding assays and chemical shift mapping indicate that a large basic patch evident on the surface of RRMs 1 and 2 is part of a high affinity U6 RNA binding site. Our results suggest that Prp24 binds free U6 RNA primarily with RRMs 1 and 2, which may remodel the U6 secondary structure. The beta-sheet of RRM 3 then influences U4/U6 pairing through interaction with an unidentified ligand.
PubMed: 17320109
DOI: 10.1016/j.jmb.2007.01.078
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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