 |
PDBsum entry 1a8y
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Calcium-binding protein
|
PDB id
|
|
|
|
1a8y
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
Nat Struct Biol
5:476-483
(1998)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum.
|
|
S.Wang,
W.R.Trumble,
H.Liao,
C.R.Wesson,
A.K.Dunker,
C.H.Kang.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
Calsequestrin, the major Ca2+ storage protein of muscle, coordinately binds and
releases 40-50 Ca2+ ions per molecule for each contraction-relaxation cycle by
an uncertain mechanism. We have determined the structure of rabbit skeletal
muscle calsequestrin. Three very negative thioredoxin-like domains surround a
hydrophilic center. Each monomer makes two extensive dimerization contacts, both
of which involve the approach of many negative groups. This structure suggests a
mechanism by which calsequestrin may achieve high capacity Ca2+ binding. The
suggested mechanism involves Ca2+-induced collapse of the three domains and
polymerization of calsequestrin monomers arising from three factors: N-terminal
arm exchange, helix-helix contacts and Ca2+ cross bridges. This proposed
structure-based mechanism accounts for the observed coupling of high capacity
Ca2+ binding with protein precipitation.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
D.H.Maclennan,
and
E.Zvaritch
(2011).
Mechanistic models for muscle diseases and disorders originating in the sarcoplasmic reticulum.
|
| |
Biochim Biophys Acta,
1813,
948-964.
|
|
|
|
|
|
|
D.W.Song,
J.G.Lee,
H.S.Youn,
S.H.Eom,
and
d.o. .H.Kim
(2011).
Ryanodine receptor assembly: A novel systems biology approach to 3D mapping.
|
| |
Prog Biophys Mol Biol,
105,
145-161.
|
|
|
|
|
|
|
G.A.Noll,
B.Müller,
A.M.Ernst,
B.Rüping,
R.M.Twyman,
and
D.Prüfer
(2011).
Native and artificial forisomes: functions and applications.
|
| |
Appl Microbiol Biotechnol,
89,
1675-1682.
|
|
|
|
|
|
|
G.Zhang,
W.Chu,
S.Hu,
T.Meng,
L.Pan,
R.Zhou,
Z.Liu,
and
J.Zhang
(2011).
Identification and Analysis of Muscle-Related Protein Isoforms Expressed in the White Muscle of the Mandarin Fish (Siniperca chuatsi).
|
| |
Mar Biotechnol (NY),
13,
151-162.
|
|
|
|
|
|
|
S.R.Shouldice,
B.Heras,
P.M.Walden,
M.Totsika,
M.A.Schembri,
and
J.L.Martin
(2011).
Structure and function of DsbA, a key bacterial oxidative folding catalyst.
|
| |
Antioxid Redox Signal,
14,
1729-1760.
|
|
|
|
|
|
|
A.Kalyanasundaram,
N.C.Bal,
C.Franzini-Armstrong,
B.C.Knollmann,
and
M.Periasamy
(2010).
The calsequestrin mutation CASQ2D307H does not affect protein stability and targeting to the junctional sarcoplasmic reticulum but compromises its dynamic regulation of calcium buffering.
|
| |
J Biol Chem,
285,
3076-3083.
|
|
|
|
|
|
|
B.Rüping,
A.M.Ernst,
S.B.Jekat,
S.Nordzieke,
A.R.Reineke,
B.Müller,
E.Bornberg-Bauer,
D.Prüfer,
and
G.A.Noll
(2010).
Molecular and phylogenetic characterization of the sieve element occlusion gene family in Fabaceae and non-Fabaceae plants.
|
| |
BMC Plant Biol,
10,
219.
|
|
|
|
|
|
|
E.Pedone,
D.Limauro,
K.D'Ambrosio,
G.De Simone,
and
S.Bartolucci
(2010).
Multiple catalytically active thioredoxin folds: a winning strategy for many functions.
|
| |
Cell Mol Life Sci,
67,
3797-3814.
|
|
|
|
|
|
|
C.Franzini-Armstrong
(2009).
Architecture and regulation of the Ca2+ delivery system in muscle cells.
|
| |
Appl Physiol Nutr Metab,
34,
323-327.
|
|
|
|
|
|
|
C.Renken,
C.E.Hsieh,
M.Marko,
B.Rath,
A.Leith,
T.Wagenknecht,
J.Frank,
and
C.A.Mannella
(2009).
Structure of frozen-hydrated triad junctions: a case study in motif searching inside tomograms.
|
| |
J Struct Biol,
165,
53-63.
|
|
|
|
|
|
|
L.Wei,
E.M.Gallant,
A.F.Dulhunty,
and
N.A.Beard
(2009).
Junctin and triadin each activate skeletal ryanodine receptors but junctin alone mediates functional interactions with calsequestrin.
|
| |
Int J Biochem Cell Biol,
41,
2214-2224.
|
|
|
|
|
|
|
N.A.Beard,
L.Wei,
and
A.F.Dulhunty
(2009).
Control of muscle ryanodine receptor calcium release channels by proteins in the sarcoplasmic reticulum lumen.
|
| |
Clin Exp Pharmacol Physiol,
36,
340-345.
|
|
|
|
|
|
|
S.H.Stoychev,
C.Nathaniel,
S.Fanucchi,
M.Brock,
S.Li,
K.Asmus,
V.L.Woods,
and
H.W.Dirr
(2009).
Structural dynamics of soluble chloride intracellular channel protein CLIC1 examined by amide hydrogen-deuterium exchange mass spectrometry.
|
| |
Biochemistry,
48,
8413-8421.
|
|
|
|
|
|
|
X.Lou,
R.Bao,
C.Z.Zhou,
and
Y.Chen
(2009).
Structure of the thioredoxin-fold domain of human phosducin-like protein 2.
|
| |
Acta Crystallogr Sect F Struct Biol Cryst Commun,
65,
67-70.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
D.Terentyev,
Z.Kubalova,
G.Valle,
A.Nori,
S.Vedamoorthyrao,
R.Terentyeva,
S.Viatchenko-Karpinski,
D.M.Bers,
S.C.Williams,
P.Volpe,
and
S.Gyorke
(2008).
Modulation of SR Ca release by luminal Ca and calsequestrin in cardiac myocytes: effects of CASQ2 mutations linked to sudden cardiac death.
|
| |
Biophys J,
95,
2037-2048.
|
|
|
|
|
|
|
S.Györke,
and
C.Carnes
(2008).
Dysregulated sarcoplasmic reticulum calcium release: potential pharmacological target in cardiac disease.
|
| |
Pharmacol Ther,
119,
340-354.
|
|
|
|
|
|
|
J.Haugstetter,
M.A.Maurer,
T.Blicher,
M.Pagac,
G.Wider,
and
L.Ellgaard
(2007).
Structure-function analysis of the endoplasmic reticulum oxidoreductase TMX3 reveals interdomain stabilization of the N-terminal redox-active domain.
|
| |
J Biol Chem,
282,
33859-33867.
|
|
|
|
|
|
|
J.L.Reyes-Juárez,
R.Juárez-Rubí,
G.Rodríguez,
and
A.Zarain-Herzberg
(2007).
Transcriptional analysis of the human cardiac calsequestrin gene in cardiac and skeletal myocytes.
|
| |
J Biol Chem,
282,
35554-35563.
|
|
|
|
|
|
|
S.Györke,
B.M.Hagen,
D.Terentyev,
and
W.J.Lederer
(2007).
Chain-reaction Ca(2+) signaling in the heart.
|
| |
J Clin Invest,
117,
1758-1762.
|
|
|
|
|
|
|
W.P.Dirksen,
V.A.Lacombe,
M.Chi,
A.Kalyanasundaram,
S.Viatchenko-Karpinski,
D.Terentyev,
Z.Zhou,
S.Vedamoorthyrao,
N.Li,
N.Chiamvimonvat,
C.A.Carnes,
C.Franzini-Armstrong,
S.Györke,
and
M.Periasamy
(2007).
A mutation in calsequestrin, CASQ2D307H, impairs Sarcoplasmic Reticulum Ca2+ handling and causes complex ventricular arrhythmias in mice.
|
| |
Cardiovasc Res,
75,
69-78.
|
|
|
|
|
|
|
A.E.Rossi,
and
R.T.Dirksen
(2006).
Sarcoplasmic reticulum: the dynamic calcium governor of muscle.
|
| |
Muscle Nerve,
33,
715-731.
|
|
|
|
|
|
|
H.Xie,
and
P.H.Zhu
(2006).
Biphasic modulation of ryanodine receptors by sulfhydryl oxidation in rat ventricular myocytes.
|
| |
Biophys J,
91,
2882-2891.
|
|
|
|
|
|
|
L.Wei,
M.Varsányi,
A.F.Dulhunty,
and
N.A.Beard
(2006).
The conformation of calsequestrin determines its ability to regulate skeletal ryanodine receptors.
|
| |
Biophys J,
91,
1288-1301.
|
|
|
|
|
|
|
S.Mkrtchian,
and
T.Sandalova
(2006).
ERp29, an unusual redox-inactive member of the thioredoxin family.
|
| |
Antioxid Redox Signal,
8,
325-337.
|
|
|
|
|
|
|
E.van Anken,
and
I.Braakman
(2005).
Versatility of the endoplasmic reticulum protein folding factory.
|
| |
Crit Rev Biochem Mol Biol,
40,
191-228.
|
|
|
|
|
|
|
N.A.Beard,
M.G.Casarotto,
L.Wei,
M.Varsányi,
D.R.Laver,
and
A.F.Dulhunty
(2005).
Regulation of ryanodine receptors by calsequestrin: effect of high luminal Ca2+ and phosphorylation.
|
| |
Biophys J,
88,
3444-3454.
|
|
|
|
|
|
|
H.Park,
I.Y.Park,
E.Kim,
B.Youn,
K.Fields,
A.K.Dunker,
and
C.Kang
(2004).
Comparing skeletal and cardiac calsequestrin structures and their calcium binding: a proposed mechanism for coupled calcium binding and protein polymerization.
|
| |
J Biol Chem,
279,
18026-18033.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
J.M.Lee,
S.H.Rho,
D.W.Shin,
C.Cho,
W.J.Park,
S.H.Eom,
J.Ma,
and
D.H.Kim
(2004).
Negatively charged amino acids within the intraluminal loop of ryanodine receptor are involved in the interaction with triadin.
|
| |
J Biol Chem,
279,
6994-7000.
|
|
|
|
|
|
|
D.W.Shin,
Z.Pan,
E.K.Kim,
J.M.Lee,
M.B.Bhat,
J.Parness,
D.H.Kim,
and
J.Ma
(2003).
A retrograde signal from calsequestrin for the regulation of store-operated Ca2+ entry in skeletal muscle.
|
| |
J Biol Chem,
278,
3286-3292.
|
|
|
|
|
|
|
H.Park,
S.Wu,
A.K.Dunker,
and
C.Kang
(2003).
Polymerization of calsequestrin. Implications for Ca2+ regulation.
|
| |
J Biol Chem,
278,
16176-16182.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
Q.Ma,
C.Guo,
K.Barnewitz,
G.M.Sheldrick,
H.D.Soling,
I.Uson,
and
D.M.Ferrari
(2003).
Crystal structure and functional analysis of Drosophila Wind, a protein-disulfide isomerase-related protein.
|
| |
J Biol Chem,
278,
44600-44607.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
A.E.Todd,
C.A.Orengo,
and
J.M.Thornton
(2002).
Sequence and structural differences between enzyme and nonenzyme homologs.
|
| |
Structure,
10,
1435-1451.
|
|
|
|
|
|
|
L.Glover,
S.Quinn,
M.Ryan,
D.Pette,
and
K.Ohlendieck
(2002).
Supramolecular calsequestrin complex.
|
| |
Eur J Biochem,
269,
4607-4616.
|
|
|
|
|
|
|
M.Eldar,
E.Pras,
and
H.Lahat
(2002).
A missense mutation in a highly conserved region of CASQ2 is associated with autosomal recessive catecholamine-induced polymorphic ventricular tachycardia in Bedouin families from Israel.
|
| |
Cold Spring Harb Symp Quant Biol,
67,
333-337.
|
|
|
|
|
|
|
N.A.Beard,
M.M.Sakowska,
A.F.Dulhunty,
and
D.R.Laver
(2002).
Calsequestrin is an inhibitor of skeletal muscle ryanodine receptor calcium release channels.
|
| |
Biophys J,
82,
310-320.
|
|
|
|
|
|
|
E.Liepinsh,
M.Baryshev,
A.Sharipo,
M.Ingelman-Sundberg,
G.Otting,
and
S.Mkrtchian
(2001).
Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer.
|
| |
Structure,
9,
457-471.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
G.Gatti,
S.Trifari,
N.Mesaeli,
J.M.Parker,
M.Michalak,
and
J.Meldolesi
(2001).
Head-to-tail oligomerization of calsequestrin: a novel mechanism for heterogeneous distribution of endoplasmic reticulum luminal proteins.
|
| |
J Cell Biol,
154,
525-534.
|
|
|
|
|
|
|
H.Lahat,
E.Pras,
T.Olender,
N.Avidan,
E.Ben-Asher,
O.Man,
E.Levy-Nissenbaum,
A.Khoury,
A.Lorber,
B.Goldman,
D.Lancet,
and
M.Eldar
(2001).
A missense mutation in a highly conserved region of CASQ2 is associated with autosomal recessive catecholamine-induced polymorphic ventricular tachycardia in Bedouin families from Israel.
|
| |
Am J Hum Genet,
69,
1378-1384.
|
|
|
|
|
|
|
D.H.MacLennan
(2000).
Ca2+ signalling and muscle disease.
|
| |
Eur J Biochem,
267,
5291-5297.
|
|
|
|
|
|
|
H.A.Lucero,
and
B.Kaminer
(1999).
The role of calcium on the activity of ERcalcistorin/protein-disulfide isomerase and the significance of the C-terminal and its calcium binding. A comparison with mammalian protein-disulfide isomerase.
|
| |
J Biol Chem,
274,
3243-3251.
|
|
|
|
|
|
|
J.Jiang,
Y.Zhang,
A.R.Krainer,
and
R.M.Xu
(1999).
Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix protein.
|
| |
Proc Natl Acad Sci U S A,
96,
3572-3577.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
D.H.MacLennan,
and
R.A.Reithmeier
(1998).
Ion tamers.
|
| |
Nat Struct Biol,
5,
409-411.
|
|
|
|
|
|
|
J.Meldolesi,
and
T.Pozzan
(1998).
The heterogeneity of ER Ca2+ stores has a key role in nonmuscle cell signaling and function.
|
| |
J Cell Biol,
142,
1395-1398.
|
|
|
|
|
|
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
code is
shown on the right.
|
|
Links
