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PDBsum entry 4jkf
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RNA binding protein
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PDB id
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4jkf
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PDB id:
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| Name: |
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RNA binding protein
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Title:
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Open and closed forms of t1791p+r1865a human prp8 rnase h-like domain with bound mg ion
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Structure:
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Pre-mRNA-processing-splicing factor 8. Chain: a, b. Fragment: prp8 rnase h-like domain, unp residues 1769-1990'. Synonym: 220 kda u5 snrnp-specific protein, prp8 homolog, splicing factor prp8, p220. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Organism_taxid: 9606. Gene: prp8, prpc8, prpf8. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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1.95Å
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R-factor:
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0.189
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R-free:
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0.226
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Authors:
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M.J.Schellenberg,T.Wu,D.B.Ritchie,K.A.Atta,A.M.Macmillan
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Key ref:
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M.J.Schellenberg
et al.
(2013).
A conformational switch in PRP8 mediates metal ion coordination that promotes pre-mRNA exon ligation.
Nat Struct Biol,
20,
728-734.
PubMed id:
DOI:
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Date:
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09-Mar-13
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Release date:
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22-May-13
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PROCHECK
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Headers
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References
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Q6P2Q9
(PRP8_HUMAN) -
Pre-mRNA-processing-splicing factor 8 from Homo sapiens
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Seq: Struc:
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2335 a.a.
220 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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DOI no:
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Nat Struct Biol
20:728-734
(2013)
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PubMed id:
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A conformational switch in PRP8 mediates metal ion coordination that promotes pre-mRNA exon ligation.
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M.J.Schellenberg,
T.Wu,
D.B.Ritchie,
S.Fica,
J.P.Staley,
K.A.Atta,
P.LaPointe,
A.M.MacMillan.
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ABSTRACT
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Splicing of pre-mRNAs in eukaryotes is catalyzed by the spliceosome, a large
RNA-protein metalloenzyme. The catalytic center of the spliceosome involves a
structure comprising the U2 and U6 snRNAs and includes a metal bound by U6
snRNA. The precise architecture of the splicesome active site, however, and the
question of whether it includes protein components, remains unresolved. A wealth
of evidence places the protein PRP8 at the heart of the spliceosome through
assembly and catalysis. Here we provide evidence that the RNase H domain of PRP8
undergoes a conformational switch between the two steps of splicing,
rationalizing yeast prp8 alleles that promote either the first or second step.
We also show that this switch unmasks a metal-binding site involved in the
second step. Together, these data establish that PRP8 is a metalloprotein that
promotes exon ligation within the spliceosome.
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');
}
}
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