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* Residue conservation analysis
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PDB id:
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Isomerase/biosynthetic protein
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Title:
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Crystal structure of a cbf5-nop10-gar1 complex
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Structure:
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Probable tRNA pseudouridine synthase b. Chain: a, b. Synonym: tRNA pseudouridine 55 synthase, psi55 synthase, tr isomerase, tRNA pseudouridylate synthase. Engineered: yes. Small nucleolar rnp similar to gar1. Chain: c, d. Engineered: yes. Ribosome biogenesis protein nop10.
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Source:
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Pyrococcus furiosus. Organism_taxid: 2261. Gene: trub. Expressed in: escherichia coli. Expression_system_taxid: 562. Organism_taxid: 186497. Strain: dsm 3638. Expression_system_taxid: 562
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Biol. unit:
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Trimer (from
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Resolution:
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2.11Å
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R-factor:
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0.211
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R-free:
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0.255
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Authors:
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R.Rashid,B.Liang,H.Li,Southeast Collaboratory For Structural (Secsg)
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Key ref:
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R.Rashid
et al.
(2006).
Crystal structure of a Cbf5-Nop10-Gar1 complex and implications in RNA-guided pseudouridylation and dyskeratosis congenita.
Mol Cell,
21,
249-260.
PubMed id:
DOI:
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Date:
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09-Nov-05
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Release date:
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24-Jan-06
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PROCHECK
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Headers
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References
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Q7LWY0
(TRUB_PYRFU) -
Probable tRNA pseudouridine synthase B
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Seq: Struc:
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340 a.a.
329 a.a.
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Enzyme class:
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Chains A, B:
E.C.5.4.99.25
- tRNA pseudouridine(55) synthase.
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Reaction:
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tRNA uridine55 = tRNA pseudouridine55
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Gene Ontology (GO) functional annotation
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Cellular component
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ribonucleoprotein complex
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2 terms
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Biological process
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ribosome biogenesis
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7 terms
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Biochemical function
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isomerase activity
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4 terms
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DOI no:
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Mol Cell
21:249-260
(2006)
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PubMed id:
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Crystal structure of a Cbf5-Nop10-Gar1 complex and implications in RNA-guided pseudouridylation and dyskeratosis congenita.
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R.Rashid,
B.Liang,
D.L.Baker,
O.A.Youssef,
Y.He,
K.Phipps,
R.M.Terns,
M.P.Terns,
H.Li.
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ABSTRACT
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H/ACA RNA-protein complexes, comprised of four proteins and an H/ACA guide RNA,
modify ribosomal and small nuclear RNAs. The H/ACA proteins are also essential
components of telomerase in mammals. Cbf5 is the H/ACA protein that catalyzes
isomerization of uridine to pseudouridine in target RNAs. Mutations in human
Cbf5 (dyskerin) lead to dyskeratosis congenita. Here, we describe the 2.1 A
crystal structure of a specific complex of three archaeal H/ACA proteins, Cbf5,
Nop10, and Gar1. Cbf5 displays structural properties that are unique among known
pseudouridine synthases and are consistent with its distinct function in
RNA-guided pseudouridylation. We also describe the previously unknown structures
of both Nop10 and Gar1 and the structural basis for their essential roles in
pseudouridylation. By using information from related structures, we have modeled
the entire ribonucleoprotein complex including both guide and substrate RNAs. We
have also identified a dyskeratosis congenita mutation cluster site within a
modeled dyskerin structure.
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Selected figure(s)
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Figure 5.
Figure 5. Comparison of Cbf5 to Regions of TruB and ArcTGT
Involved in RNA Binding
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Figure 6.
Figure 6. Structural Model of Fully Assembled H/ACA RNP
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2006,
21,
249-260)
copyright 2006.
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Figures were
selected
by the author.
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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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B.Liang,
and
H.Li
(2011).
Structures of ribonucleoprotein particle modification enzymes.
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Q Rev Biophys, 44,
95.
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B.W.Gu,
J.M.Fan,
M.Bessler,
and
P.J.Mason
(2011).
Accelerated hematopoietic stem cell aging in a mouse model of dyskeratosis congenita responds to antioxidant treatment.
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Aging Cell, 10,
338-348.
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C.Trahan,
C.Martel,
and
F.Dragon
(2010).
Effects of dyskeratosis congenita mutations in dyskerin, NHP2 and NOP10 on assembly of H/ACA pre-RNPs.
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Hum Mol Genet, 19,
825-836.
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T.Hamma,
and
A.R.Ferré-D'Amaré
(2010).
The box H/ACA ribonucleoprotein complex: interplay of RNA and protein structures in post-transcriptional RNA modification.
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J Biol Chem, 285,
805-809.
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T.Kiss,
E.Fayet-Lebaron,
and
B.E.Jády
(2010).
Box H/ACA small ribonucleoproteins.
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Mol Cell, 37,
597-606.
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B.Ashbridge,
A.Orte,
J.A.Yeoman,
M.Kirwan,
T.Vulliamy,
I.Dokal,
D.Klenerman,
and
S.Balasubramanian
(2009).
Single-molecule analysis of the human telomerase RNA.dyskerin interaction and the effect of dyskeratosis congenita mutations.
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Biochemistry, 48,
10858-10865.
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B.Liang,
J.Zhou,
E.Kahen,
R.M.Terns,
M.P.Terns,
and
H.Li
(2009).
Structure of a functional ribonucleoprotein pseudouridine synthase bound to a substrate RNA.
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Nat Struct Mol Biol, 16,
740-746.
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PDB codes:
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J.Donovan,
and
P.R.Copeland
(2009).
Evolutionary history of selenocysteine incorporation from the perspective of SECIS binding proteins.
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BMC Evol Biol, 9,
229.
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J.He,
B.W.Gu,
J.Ge,
Y.Mochizuki,
M.Bessler,
and
P.J.Mason
(2009).
Variable expression of Dkc1 mutations in mice.
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Genesis, 47,
366-373.
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J.R.Zamudio,
B.Mittra,
A.Chattopadhyay,
J.A.Wohlschlegel,
N.R.Sturm,
and
D.A.Campbell
(2009).
Trypanosoma brucei spliced leader RNA maturation by the cap 1 2'-O-ribose methyltransferase and SLA1 H/ACA snoRNA pseudouridine synthase complex.
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Mol Cell Biol, 29,
1202-1211.
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M.Kirwan,
and
I.Dokal
(2009).
Dyskeratosis congenita, stem cells and telomeres.
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Biochim Biophys Acta, 1792,
371-379.
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P.N.Grozdanov,
N.Fernandez-Fuentes,
A.Fiser,
and
U.T.Meier
(2009).
Pathogenic NAP57 mutations decrease ribonucleoprotein assembly in dyskeratosis congenita.
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Hum Mol Genet, 18,
4546-4551.
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P.N.Grozdanov,
S.Roy,
N.Kittur,
and
U.T.Meier
(2009).
SHQ1 is required prior to NAF1 for assembly of H/ACA small nucleolar and telomerase RNPs.
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RNA, 15,
1188-1197.
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S.Pigullo,
E.Pavesi,
I.Dianzani,
G.Santamaria,
J.Svahn,
M.Risso,
M.T.Van Lint,
M.Pillon,
A.P.Iori,
D.Longoni,
U.Ramenghi,
M.Lanciotti,
and
C.Dufour
(2009).
NOLA1 gene mutations in acquired aplastic anemia.
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Pediatr Blood Cancer, 52,
376-378.
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B.Liang,
E.J.Kahen,
K.Calvin,
J.Zhou,
M.Blanco,
and
H.Li
(2008).
Long-distance placement of substrate RNA by H/ACA proteins.
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RNA, 14,
2086-2094.
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H.Li
(2008).
Unveiling substrate RNA binding to H/ACA RNPs: one side fits all.
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Curr Opin Struct Biol, 18,
78-85.
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J.Karijolich,
and
Y.T.Yu
(2008).
Insight into the Protein Components of the Box H/ACA RNP.
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Curr Proteomics, 5,
129-137.
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K.Collins
(2008).
Physiological assembly and activity of human telomerase complexes.
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Mech Ageing Dev, 129,
91-98.
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K.Kannan,
A.D.Nelson,
and
D.E.Shippen
(2008).
Dyskerin is a component of the Arabidopsis telomerase RNP required for telomere maintenance.
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Mol Cell Biol, 28,
2332-2341.
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L.Tang,
A.Sahasranaman,
J.Jakovljevic,
E.Schleifman,
and
J.L.Woolford
(2008).
Interactions among Ytm1, Erb1, and Nop7 required for assembly of the Nop7-subcomplex in yeast preribosomes.
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Mol Biol Cell, 19,
2844-2856.
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M.Kirwan,
and
I.Dokal
(2008).
Dyskeratosis congenita: a genetic disorder of many faces.
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Clin Genet, 73,
103-112.
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R.Ishitani,
S.Yokoyama,
and
O.Nureki
(2008).
Structure, dynamics, and function of RNA modification enzymes.
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Curr Opin Struct Biol, 18,
330-339.
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R.Machado-Pinilla,
I.Sánchez-Pérez,
J.R.Murguía,
L.Sastre,
and
R.Perona
(2008).
A dyskerin motif reactivates telomerase activity in X-linked dyskeratosis congenita and in telomerase-deficient human cells.
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Blood, 111,
2606-2614.
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S.Muller,
F.Leclerc,
I.Behm-Ansmant,
J.B.Fourmann,
B.Charpentier,
and
C.Branlant
(2008).
Combined in silico and experimental identification of the Pyrococcus abyssi H/ACA sRNAs and their target sites in ribosomal RNAs.
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Nucleic Acids Res, 36,
2459-2475.
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T.Vulliamy,
R.Beswick,
M.Kirwan,
A.Marrone,
M.Digweed,
A.Walne,
and
I.Dokal
(2008).
Mutations in the telomerase component NHP2 cause the premature ageing syndrome dyskeratosis congenita.
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Proc Natl Acad Sci U S A, 105,
8073-8078.
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W.A.Decatur,
and
M.N.Schnare
(2008).
Different mechanisms for pseudouridine formation in yeast 5S and 5.8S rRNAs.
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Mol Cell Biol, 28,
3089-3100.
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A.G.Matera,
R.M.Terns,
and
M.P.Terns
(2007).
Non-coding RNAs: lessons from the small nuclear and small nucleolar RNAs.
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Nat Rev Mol Cell Biol, 8,
209-220.
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A.J.Walne,
T.Vulliamy,
A.Marrone,
R.Beswick,
M.Kirwan,
Y.Masunari,
F.H.Al-Qurashi,
M.Aljurf,
and
I.Dokal
(2007).
Genetic heterogeneity in autosomal recessive dyskeratosis congenita with one subtype due to mutations in the telomerase-associated protein NOP10.
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Hum Mol Genet, 16,
1619-1629.
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C.K.Garcia,
W.E.Wright,
and
J.W.Shay
(2007).
Human diseases of telomerase dysfunction: insights into tissue aging.
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Nucleic Acids Res, 35,
7406-7416.
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H.Jin,
J.P.Loria,
and
P.B.Moore
(2007).
Solution structure of an rRNA substrate bound to the pseudouridylation pocket of a box H/ACA snoRNA.
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Mol Cell, 26,
205-215.
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PDB codes:
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H.Wu,
and
J.Feigon
(2007).
H/ACA small nucleolar RNA pseudouridylation pockets bind substrate RNA to form three-way junctions that position the target U for modification.
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Proc Natl Acad Sci U S A, 104,
6655-6660.
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PDB code:
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I.Pérez-Arellano,
J.Gallego,
and
J.Cervera
(2007).
The PUA domain - a structural and functional overview.
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FEBS J, 274,
4972-4984.
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J.de la Fuente,
and
I.Dokal
(2007).
Dyskeratosis congenita: advances in the understanding of the telomerase defect and the role of stem cell transplantation.
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Pediatr Transplant, 11,
584-594.
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K.Ye
(2007).
H/ACA guide RNAs, proteins and complexes.
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Curr Opin Struct Biol, 17,
287-292.
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S.Hur,
and
R.M.Stroud
(2007).
How U38, 39, and 40 of many tRNAs become the targets for pseudouridylation by TruA.
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Mol Cell, 26,
189-203.
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PDB codes:
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S.L.Reichow,
T.Hamma,
A.R.Ferré-D'Amaré,
and
G.Varani
(2007).
The structure and function of small nucleolar ribonucleoproteins.
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Nucleic Acids Res, 35,
1452-1464.
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S.Muller,
J.B.Fourmann,
C.Loegler,
B.Charpentier,
and
C.Branlant
(2007).
Identification of determinants in the protein partners aCBF5 and aNOP10 necessary for the tRNA:Psi55-synthase and RNA-guided RNA:Psi-synthase activities.
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Nucleic Acids Res, 35,
5610-5624.
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S.Riccardo,
G.Tortoriello,
E.Giordano,
M.Turano,
and
M.Furia
(2007).
The coding/non-coding overlapping architecture of the gene encoding the Drosophila pseudouridine synthase.
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BMC Mol Biol, 8,
15.
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S.Suzuki,
A.Tatsuguchi,
E.Matsumoto,
M.Kawazoe,
T.Kaminishi,
M.Shirouzu,
Y.Muto,
C.Takemoto,
and
S.Yokoyama
(2007).
Structural characterization of the ribosome maturation protein, RimM.
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J Bacteriol, 189,
6397-6406.
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PDB code:
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C.A.Theimer,
and
J.Feigon
(2006).
Structure and function of telomerase RNA.
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Curr Opin Struct Biol, 16,
307-318.
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C.Normand,
R.Capeyrou,
S.Quevillon-Cheruel,
A.Mougin,
Y.Henry,
and
M.Caizergues-Ferrer
(2006).
Analysis of the binding of the N-terminal conserved domain of yeast Cbf5p to a box H/ACA snoRNA.
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RNA, 12,
1868-1882.
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D.C.Zappulla,
and
T.R.Cech
(2006).
RNA as a flexible scaffold for proteins: yeast telomerase and beyond.
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Cold Spring Harb Symp Quant Biol, 71,
217-224.
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F.van den Ent,
M.Leaver,
F.Bendezu,
J.Errington,
P.de Boer,
and
J.Löwe
(2006).
Dimeric structure of the cell shape protein MreC and its functional implications.
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Mol Microbiol, 62,
1631-1642.
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PDB code:
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L.Li,
and
K.Ye
(2006).
Crystal structure of an H/ACA box ribonucleoprotein particle.
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Nature, 443,
302-307.
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PDB code:
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M.Roovers,
C.Hale,
C.Tricot,
M.P.Terns,
R.M.Terns,
H.Grosjean,
and
L.Droogmans
(2006).
Formation of the conserved pseudouridine at position 55 in archaeal tRNA.
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Nucleic Acids Res, 34,
4293-4301.
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M.Terns,
and
R.Terns
(2006).
Noncoding RNAs of the H/ACA family.
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Cold Spring Harb Symp Quant Biol, 71,
395-405.
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N.Kittur,
X.Darzacq,
S.Roy,
R.H.Singer,
and
U.T.Meier
(2006).
Dynamic association and localization of human H/ACA RNP proteins.
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RNA, 12,
2057-2062.
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S.Hur,
R.M.Stroud,
and
J.Finer-Moore
(2006).
Substrate recognition by RNA 5-methyluridine methyltransferases and pseudouridine synthases: a structural perspective.
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J Biol Chem, 281,
38969-38973.
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U.T.Meier
(2006).
How a single protein complex accommodates many different H/ACA RNAs.
|
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Trends Biochem Sci, 31,
311-315.
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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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