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PDBsum entry 4jkf

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protein metals Protein-protein interface(s) links
RNA binding protein PDB id
4jkf

 

 

 

 

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Contents
Protein chains
220 a.a.
Metals
_MG
Waters ×437
PDB id:
4jkf
Name: RNA binding protein
Title: Open and closed forms of t1791p+r1865a human prp8 rnase h-like domain with bound mg ion
Structure: 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
Source: Homo sapiens. Organism_taxid: 9606. Gene: prp8, prpc8, prpf8. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.95Å     R-factor:   0.189     R-free:   0.226
Authors: M.J.Schellenberg,T.Wu,D.B.Ritchie,K.A.Atta,A.M.Macmillan
Key ref: 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: 23686287 DOI: 10.1038/nsmb.2556
Date:
09-Mar-13     Release date:   22-May-13    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q6P2Q9  (PRP8_HUMAN) -  Pre-mRNA-processing-splicing factor 8 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2335 a.a.
220 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 

 
DOI no: 10.1038/nsmb.2556 Nat Struct Biol 20:728-734 (2013)
PubMed id: 23686287  
 
 
A conformational switch in PRP8 mediates metal ion coordination that promotes pre-mRNA exon ligation.
M.J.Schellenberg, T.Wu, D.B.Ritchie, S.Fica, J.P.Staley, K.A.Atta, P.LaPointe, A.M.MacMillan.
 
  ABSTRACT  
 
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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