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RNA binding protein
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PDB id
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1mp1
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Contents |
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* Residue conservation analysis
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PDB id:
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RNA binding protein
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Title:
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Solution structure of the pwi motif from srm160
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Structure:
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Ser/arg-related nuclear matrix protein. Chain: a. Fragment: pwi motif (residues 27-134). Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: srm160. Expressed in: escherichia coli. Expression_system_taxid: 562.
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NMR struc:
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20 models
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Authors:
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B.R.Szymczyna,J.Bowman,S.Mccracken,A.Pineda-Lucena,Y.Lu, B.Cox,M.Lambermon,B.R.Graveley,C.H.Arrowsmith,B.J.Blencowe
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Key ref:
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B.R.Szymczyna
et al.
(2003).
Structure and function of the PWI motif: a novel nucleic acid-binding domain that facilitates pre-mRNA processing.
Genes Dev,
17,
461-475.
PubMed id:
DOI:
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Date:
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11-Sep-02
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Release date:
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16-Sep-03
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PROCHECK
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Headers
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References
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Q8IYB3
(SRRM1_HUMAN) -
Serine/arginine repetitive matrix protein 1
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Seq: Struc:
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904 a.a.
111 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 3 residue positions (black
crosses)
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Gene Ontology (GO) functional annotation
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Biological process
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mRNA processing
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1 term
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DOI no:
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Genes Dev
17:461-475
(2003)
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PubMed id:
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Structure and function of the PWI motif: a novel nucleic acid-binding domain that facilitates pre-mRNA processing.
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B.R.Szymczyna,
J.Bowman,
S.McCracken,
A.Pineda-Lucena,
Y.Lu,
B.Cox,
M.Lambermon,
B.R.Graveley,
C.H.Arrowsmith,
B.J.Blencowe.
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ABSTRACT
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The PWI motif is a highly conserved domain of unknown function in the SRm160
splicing and 3'-end cleavage-stimulatory factor, as well as in several other
known or putative pre-mRNA processing components. We show here that the PWI
motif is a new type of RNA/DNA-binding domain that has an equal preference for
single- and double-stranded nucleic acids. Deletion of the motif prevents SRm160
from binding RNA and stimulating 3'-end cleavage, and its substitution with a
heterologous RNA-binding domain restores these functions. The NMR solution
structure of the SRm160-PWI motif reveals a novel, four-helix bundle and
represents the first example of an alpha-helical fold that can bind
single-stranded (ss)RNA. Structure-guided mutagenesis indicates that the same
surface is involved in RNA and DNA binding and requires the cooperative action
of a highly conserved, adjacent basic region. Thus, the PWI motif is a novel
type of nucleic acid-binding domain that likely has multiple important functions
in pre-mRNA processing, including SRm160-dependent stimulation of 3'-end
formation.
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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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K.B.Cook,
H.Kazan,
K.Zuberi,
Q.Morris,
and
T.R.Hughes
(2011).
RBPDB: a database of RNA-binding specificities.
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Nucleic Acids Res, 39,
D301-D308.
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R.Tuteja,
and
J.Mehta
(2010).
A genomic glance at the components of the mRNA export machinery in Plasmodium falciparum.
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Commun Integr Biol, 3,
318-326.
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S.Millevoi,
and
S.Vagner
(2010).
Molecular mechanisms of eukaryotic pre-mRNA 3' end processing regulation.
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Nucleic Acids Res, 38,
2757-2774.
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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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M.B.Fasken,
M.Stewart,
and
A.H.Corbett
(2008).
Functional significance of the interaction between the mRNA-binding protein, Nab2, and the nuclear pore-associated protein, Mlp1, in mRNA export.
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J Biol Chem, 283,
27130-27143.
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R.P.Grant,
N.J.Marshall,
J.C.Yang,
M.B.Fasken,
S.M.Kelly,
M.T.Harreman,
D.Neuhaus,
A.H.Corbett,
and
M.Stewart
(2008).
Structure of the N-terminal Mlp1-binding domain of the Saccharomyces cerevisiae mRNA-binding protein, Nab2.
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J Mol Biol, 376,
1048-1059.
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PDB codes:
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D.H.Parry,
J.Xu,
and
G.Ruvkun
(2007).
A whole-genome RNAi Screen for C. elegans miRNA pathway genes.
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Curr Biol, 17,
2013-2022.
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J.Qiu,
F.Cheng,
and
D.Pintel
(2007).
Distance-dependent processing of adeno-associated virus type 5 RNA is controlled by 5' exon definition.
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J Virol, 81,
7974-7984.
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K.Kuwasako,
F.He,
M.Inoue,
A.Tanaka,
S.Sugano,
P.Güntert,
Y.Muto,
and
S.Yokoyama
(2006).
Solution structures of the SURP domains and the subunit-assembly mechanism within the splicing factor SF3a complex in 17S U2 snRNP.
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Structure, 14,
1677-1689.
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PDB codes:
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A.F.Yakunin,
A.A.Yee,
A.Savchenko,
A.M.Edwards,
and
C.H.Arrowsmith
(2004).
Structural proteomics: a tool for genome annotation.
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Curr Opin Chem Biol, 8,
42-48.
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J.Medenbach,
S.Schreiner,
S.Liu,
R.Lührmann,
and
A.Bindereif
(2004).
Human U4/U6 snRNP recycling factor p110: mutational analysis reveals the function of the tetratricopeptide repeat domain in recycling.
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Mol Cell Biol, 24,
7392-7401.
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M.McLaren,
K.Asai,
and
A.Cochrane
(2004).
A novel function for Sam68: enhancement of HIV-1 RNA 3' end processing.
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RNA, 10,
1119-1129.
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V.Anantharaman,
and
L.Aravind
(2004).
Novel conserved domains in proteins with predicted roles in eukaryotic cell-cycle regulation, decapping and RNA stability.
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BMC Genomics, 5,
45.
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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.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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