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* Residue conservation analysis
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PDB id:
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Cell cycle
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Title:
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Crystal structure of sfi1p/cdc31p complex
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Structure:
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Cell division control protein 31. Chain: a, b, d, e. Synonym: nucleoporin cdc31, nuclear pore protein cdc31. Engineered: yes. Sfi1p. Chain: c, f. Fragment: residues: 643-710. Engineered: yes
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: cdc31. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: sfi1.
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Biol. unit:
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Trimer (from
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Resolution:
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3.00Å
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R-factor:
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0.255
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R-free:
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0.297
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Authors:
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S.Li,A.M.Sandercock,P.T.Conduit,C.V.Robinson,R.L.Williams, J.V.Kilmartin
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Key ref:
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S.Li
et al.
(2006).
Structural role of Sfi1p-centrin filaments in budding yeast spindle pole body duplication.
J Cell Biol,
173,
867-877.
PubMed id:
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Date:
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02-May-06
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Release date:
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27-Jun-06
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PROCHECK
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Headers
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References
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J Cell Biol
173:867-877
(2006)
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PubMed id:
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Structural role of Sfi1p-centrin filaments in budding yeast spindle pole body duplication.
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S.Li,
A.M.Sandercock,
P.Conduit,
C.V.Robinson,
R.L.Williams,
J.V.Kilmartin.
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ABSTRACT
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Centrins are calmodulin-like proteins present in centrosomes and yeast spindle
pole bodies (SPBs) and have essential functions in their duplication. The
Saccharomyces cerevisiae centrin, Cdc31p, binds Sfi1p on multiple conserved
repeats; both proteins localize to the SPB half-bridge, where the new SPB is
assembled. The crystal structures of Sfi1p-centrin complexes containing several
repeats show Sfi1p as an alpha helix with centrins wrapped around each repeat
and similar centrin-centrin contacts between each repeat. Electron microscopy
(EM) shadowing of an Sfi1p-centrin complex with 15 Sfi1 repeats and 15 centrins
bound showed filaments 60 nm long, compatible with all the Sfi1 repeats as a
continuous alpha helix. Immuno-EM localization of the Sfi1p N and C termini
showed Sfi1p-centrin filaments spanning the length of the half-bridge with the
Sfi1p N terminus at the SPB. This suggests a model for SPB duplication where the
half-bridge doubles in length by association of the Sfi1p C termini, thereby
providing a new Sfi1p N terminus to initiate SPB assembly.
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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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N.Tanaka,
M.Goto,
A.Kawasaki,
T.Sasano,
K.Eto,
R.Nishi,
K.Sugasawa,
S.Abe,
and
H.Saitoh
(2010).
An EF-hands protein, centrin-1, is an EGTA-sensitive SUMO-interacting protein in mouse testis.
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Cell Biochem Funct,
28,
604-612.
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Y.Araki,
L.Gombos,
S.P.Migueleti,
L.Sivashanmugam,
C.Antony,
and
E.Schiebel
(2010).
N-terminal regions of Mps1 kinase determine functional bifurcation.
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J Cell Biol,
189,
41-56.
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D.Jani,
S.Lutz,
N.J.Marshall,
T.Fischer,
A.Köhler,
A.M.Ellisdon,
E.Hurt,
and
M.Stewart
(2009).
Sus1, Cdc31, and the Sac3 CID region form a conserved interaction platform that promotes nuclear pore association and mRNA export.
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Mol Cell,
33,
727-737.
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PDB codes:
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H.H.Lim,
T.Zhang,
and
U.Surana
(2009).
Regulation of centrosome separation in yeast and vertebrates: common threads.
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Trends Cell Biol,
19,
325-333.
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J.Azimzadeh,
P.Hergert,
A.Delouvée,
U.Euteneuer,
E.Formstecher,
A.Khodjakov,
and
M.Bornens
(2009).
hPOC5 is a centrin-binding protein required for assembly of full-length centrioles.
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J Cell Biol,
185,
101-114.
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P.Melloy,
S.Shen,
E.White,
and
M.D.Rose
(2009).
Distinct roles for key karyogamy proteins during yeast nuclear fusion.
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Mol Biol Cell,
20,
3773-3782.
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E.Alfaro,
L.d.e.l. .V.Sosa,
Z.Sanoguet,
B.Pastrana-Ríos,
and
E.R.Schreiter
(2008).
Crystallization and preliminary X-ray characterization of full-length Chlamydomonas reinhardtii centrin.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
64,
402-404.
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J.L.Salisbury
(2008).
Breaking the ties that bind centriole numbers.
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Nat Cell Biol,
10,
255-257.
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K.K.Resendes,
B.A.Rasala,
and
D.J.Forbes
(2008).
Centrin 2 localizes to the vertebrate nuclear pore and plays a role in mRNA and protein export.
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Mol Cell Biol,
28,
1755-1769.
|
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L.A.Simmons Kovacs,
C.L.Nelson,
and
S.B.Haase
(2008).
Intrinsic and cyclin-dependent kinase-dependent control of spindle pole body duplication in budding yeast.
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Mol Biol Cell,
19,
3243-3253.
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L.Chen,
and
K.Madura
(2008).
Centrin/Cdc31 is a novel regulator of protein degradation.
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Mol Cell Biol,
28,
1829-1840.
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M.Bornens
(2008).
Organelle positioning and cell polarity.
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Nat Rev Mol Cell Biol,
9,
874-886.
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P.Strnad,
and
P.Gönczy
(2008).
Mechanisms of procentriole formation.
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Trends Cell Biol,
18,
389-396.
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P.Trojan,
N.Krauss,
H.W.Choe,
A.Giessl,
A.Pulvermüller,
and
U.Wolfrum
(2008).
Centrins in retinal photoreceptor cells: regulators in the connecting cilium.
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Prog Retin Eye Res,
27,
237-259.
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D.Gogendeau,
J.Beisson,
N.G.de Loubresse,
J.P.Le Caer,
F.Ruiz,
J.Cohen,
L.Sperling,
F.Koll,
and
C.Klotz
(2007).
An Sfi1p-like centrin-binding protein mediates centrin-based Ca2+ -dependent contractility in Paramecium tetraurelia.
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Eukaryot Cell,
6,
1992-2000.
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J.L.Salisbury
(2007).
A mechanistic view on the evolutionary origin for centrin-based control of centriole duplication.
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J Cell Physiol,
213,
420-428.
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M.Bettencourt-Dias,
and
D.M.Glover
(2007).
Centrosome biogenesis and function: centrosomics brings new understanding.
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Nat Rev Mol Cell Biol,
8,
451-463.
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P.Melloy,
S.Shen,
E.White,
J.R.McIntosh,
and
M.D.Rose
(2007).
Nuclear fusion during yeast mating occurs by a three-step pathway.
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J Cell Biol,
179,
659-670.
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V.E.Anderson,
J.Prudden,
S.Prochnik,
T.H.Giddings,
and
K.G.Hardwick
(2007).
Novel sfi1 alleles uncover additional functions for Sfi1p in bipolar spindle assembly and function.
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Mol Biol Cell,
18,
2047-2056.
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Y.Blouquit,
P.Duchambon,
E.Brun,
S.Marco,
F.Rusconi,
and
C.Sicard-Roselli
(2007).
High sensitivity of human centrin 2 toward radiolytical oxidation: C-terminal tyrosinyl residue as the main target.
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Free Radic Biol Med,
43,
216-228.
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K.Crasta,
and
U.Surana
(2006).
Disjunction of conjoined twins: Cdk1, Cdh1 and separation of centrosomes.
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Cell Div,
1,
12.
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|
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|
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L.A.Strawn,
and
H.L.True
(2006).
Deletion of RNQ1 gene reveals novel functional relationship between divergently transcribed Bik1p/CLIP-170 and Sfi1p in spindle pole body separation.
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Curr Genet,
50,
347-366.
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S.L.Jaspersen,
A.E.Martin,
G.Glazko,
T.H.Giddings,
G.Morgan,
A.Mushegian,
and
M.Winey
(2006).
The Sad1-UNC-84 homology domain in Mps3 interacts with Mps2 to connect the spindle pole body with the nuclear envelope.
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J Cell Biol,
174,
665-675.
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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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}
}
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