 |
PDBsum entry 4jkf
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
RNA binding protein
|
PDB id
|
|
|
|
4jkf
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
A conformational switch in prp8 mediates metal ion coordination that promotes pre-Mrna exon ligation.
|
 |
|
Authors
|
 |
M.J.Schellenberg,
T.Wu,
D.B.Ritchie,
S.Fica,
J.P.Staley,
K.A.Atta,
P.Lapointe,
A.M.Macmillan.
|
 |
|
Ref.
|
 |
Nat Struct Biol, 2013,
20,
728-734.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
|
|
 |
 |
|
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.
|
 |
|
|
|
|
 |