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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Crystal structure of a truncated human tudor-sn
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Structure:
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Staphylococcal nuclease domain-containing protein 1. Chain: a. Fragment: tsn-64 (sn3, sn4, tudor, sn5 domains). Synonym: tudor-sn, p100 co-activator, 100 kda coactivator, ebna2 coactivator p100, tudor domain-containing protein 11. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: snd1, tdrd11. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.90Å
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R-factor:
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0.175
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R-free:
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0.209
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Authors:
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C.L.Li
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Key ref:
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C.L.Li
et al.
(2008).
Structural and functional insights into human Tudor-SN, a key component linking RNA interference and editing.
Nucleic Acids Res,
36,
3579-3589.
PubMed id:
DOI:
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Date:
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15-Nov-07
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Release date:
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26-Aug-08
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PROCHECK
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Headers
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References
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Q7KZF4
(SND1_HUMAN) -
Staphylococcal nuclease domain-containing protein 1
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Seq:
Struc:
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910 a.a.
537 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Gene Ontology (GO) functional annotation
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Biochemical function
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nucleic acid binding
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2 terms
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DOI no:
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Nucleic Acids Res
36:3579-3589
(2008)
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PubMed id:
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Structural and functional insights into human Tudor-SN, a key component linking RNA interference and editing.
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C.L.Li,
W.Z.Yang,
Y.P.Chen,
H.S.Yuan.
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ABSTRACT
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Human Tudor-SN is involved in the degradation of hyper-edited inosine-containing
microRNA precursors, thus linking the pathways of RNA interference and editing.
Tudor-SN contains four tandem repeats of staphylococcal nuclease-like domains
(SN1-SN4) followed by a tudor and C-terminal SN domain (SN5). Here, we showed
that Tudor-SN requires tandem repeats of SN domains for its RNA binding and
cleavage activity. The crystal structure of a 64-kD truncated form of human
Tudor-SN further shows that the four domains, SN3, SN4, tudor and SN5, assemble
into a crescent-shaped structure. A concave basic surface formed jointly by SN3
and SN4 domains is likely involved in RNA binding, where citrate ions are bound
at the putative RNase active sites. Additional modeling studies provide a
structural basis for Tudor-SN's preference in cleaving RNA containing multiple
I.U wobble-paired sequences. Collectively, these results suggest that tandem
repeats of SN domains in Tudor-SN function as a clamp to capture RNA substrates.
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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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Y.Lei,
Y.Huang,
H.Zhang,
L.Yu,
M.Zhang,
and
A.Dayton
(2011).
Functional interaction between cellular p100 and the dengue virus 3' UTR.
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J Gen Virol, 92,
796-806.
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J.Kraut-Cohen,
and
J.E.Gerst
(2010).
Addressing mRNAs to the ER: cis sequences act up!
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Trends Biochem Sci, 35,
459-469.
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J.Lu,
J.Zheng,
H.Liu,
J.Li,
H.Chen,
and
K.Chen
(2010).
Protein profiling analysis of skeletal muscle of a pufferfish, Takifugu rubripes.
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Mol Biol Rep, 37,
2141-2147.
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K.Liu,
C.Chen,
Y.Guo,
R.Lam,
C.Bian,
C.Xu,
D.Y.Zhao,
J.Jin,
F.MacKenzie,
T.Pawson,
and
J.Min
(2010).
Structural basis for recognition of arginine methylated Piwi proteins by the extended Tudor domain.
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Proc Natl Acad Sci U S A, 107,
18398-18403.
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PDB codes:
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J.Zheng,
J.Lu,
H.Liu,
J.Li,
and
K.Chen
(2009).
Sequence and structural analysis of 4SNc-Tudor domain protein from Takifugu Rubripes.
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Bioinformation, 4,
127-131.
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K.Paukku,
N.Kalkkinen,
O.Silvennoinen,
K.K.Kontula,
and
J.Y.Lehtonen
(2008).
p100 increases AT1R expression through interaction with AT1R 3'-UTR.
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Nucleic Acids Res, 36,
4474-4487.
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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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Links
