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PDBsum entry 2jkd
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Gene regulation
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PDB id
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2jkd
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Gene regulation
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Title:
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Structure of the yeast pml1 splicing factor and its integration into the res complex
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Structure:
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Pre-mRNA leakage protein 1. Chain: a, b. Fragment: fha domain, residues 25-204. Synonym: pml1. Engineered: yes
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Strain: s288c. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.50Å
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R-factor:
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0.217
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R-free:
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0.262
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Authors:
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M.A.Brooks,A.Dziembowski,S.Quevillon-Cheruel,V.Henriot,C.Faux,H.Van Tilbeurgh,B.Seraphin
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Key ref:
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M.A.Brooks
et al.
(2009).
Structure of the yeast Pml1 splicing factor and its integration into the RES complex.
Nucleic Acids Res,
37,
129-143.
PubMed id:
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Date:
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27-Aug-08
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Release date:
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26-Sep-08
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PROCHECK
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Headers
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References
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Q07930
(PML1_YEAST) -
Pre-mRNA leakage protein 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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204 a.a.
150 a.a.
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Key: |
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Secondary structure |
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CATH domain |
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Nucleic Acids Res
37:129-143
(2009)
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PubMed id:
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Structure of the yeast Pml1 splicing factor and its integration into the RES complex.
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M.A.Brooks,
A.Dziembowski,
S.Quevillon-Cheruel,
V.Henriot,
C.Faux,
H.van Tilbeurgh,
B.Séraphin.
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ABSTRACT
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The RES complex was previously identified in yeast as a splicing factor
affecting nuclear pre-mRNA retention. This complex was shown to contain three
subunits, namely Snu17, Bud13 and Pml1, but its mode of action remains
ill-defined. To obtain insights into its function, we have performed a
structural investigation of this factor. Production of a short N-terminal
truncation of residues that are apparently disordered allowed us to determine
the X-ray crystallographic structure of Pml1. This demonstrated that it consists
mainly of a FHA domain, a fold which has been shown to mediate interactions with
phosphothreonine-containing peptides. Using a new sensitive assay based on
alternative splice-site choice, we show, however, that mutation of the putative
phosphothreonine-binding pocket of Pml1 does not affect pre-mRNA splicing. We
have also investigated how Pml1 integrates into the RES complex. Production of
recombinant complexes, combined with serial truncation and mutagenesis of their
subunits, indicated that Pml1 binds to Snu17, which itself contacts Bud13. This
analysis allowed us to demarcate the binding sites involved in the formation of
this assembly. We propose a model of the organization of the RES complex based
on these results, and discuss the functional consequences of this architecture.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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M.Khanna,
H.Van Bakel,
X.Tang,
J.A.Calarco,
T.Babak,
G.Guo,
A.Emili,
J.F.Greenblatt,
T.R.Hughes,
N.J.Krogan,
and
B.J.Blencowe
(2009).
A systematic characterization of Cwc21, the yeast ortholog of the human spliceosomal protein SRm300.
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RNA,
15,
2174-2185.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
