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PDBsum entry 1hce
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Actin binding
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PDB id
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1hce
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Nature
359:855-858
(1992)
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PubMed id:
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Structure of hisactophilin is similar to interleukin-1 beta and fibroblast growth factor.
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J.Habazettl,
D.Gondol,
R.Wiltscheck,
J.Otlewski,
M.Schleicher,
T.A.Holak.
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ABSTRACT
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The fast reaction of the actin-based cytoskeleton in motile cells after
stimulation with a chemoattractant requires a signal-transduction chain that
creates a very specific environment at distinct regions beneath the plasma
membrane. Dictyostelium hisactophilin, a unique actin-binding protein, is a
submembranous pH sensor that signals slight changes of the H+ concentration to
actin by inducing actin polymerization and binding to microfilaments only at pH
values below seven. It has a relative molecular mass of 13.5K and its most
unusual feature is the presence of 31 histidine residues among its total of 118
amino acids. The transduction of an external signal from the plasma membrane to
the cytoskeleton is poorly understood. Here we report the protein's structure in
solution determined by nuclear magnetic resonance spectroscopy. The nuclear
Overhauser effect intensities of the three-dimensional nuclear Overhauser
spectra were used directly in the calculations. The overall folding of
histactophilin is similar to that of interleukin-1 beta and fibroblast growth
factor, but the primary amino-acid sequence of hisactophilin is unrelated to
these two proteins.
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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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M.Schleicher,
and
B.M.Jockusch
(2008).
Actin: its cumbersome pilgrimage through cellular compartments.
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Histochem Cell Biol,
129,
695-704.
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N.Kulahin,
V.Kiselyov,
A.Kochoyan,
O.Kristensen,
J.S.Kastrup,
V.Berezin,
E.Bock,
and
M.Gajhede
(2007).
Structure of rat acidic fibroblast growth factor at 1.4 A resolution.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
63,
65-68.
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PDB code:
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L.L.Chavez,
S.Gosavi,
P.A.Jennings,
and
J.N.Onuchic
(2006).
Multiple routes lead to the native state in the energy landscape of the beta-trefoil family.
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Proc Natl Acad Sci U S A,
103,
10254-10258.
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E.A.Nordahl,
V.Rydengård,
M.Mörgelin,
and
A.Schmidtchen
(2005).
Domain 5 of high molecular weight kininogen is antibacterial.
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J Biol Chem,
280,
34832-34839.
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J.M.Mancheño,
H.Tateno,
I.J.Goldstein,
M.Martínez-Ripoll,
and
J.A.Hermoso
(2005).
Structural analysis of the Laetiporus sulphureus hemolytic pore-forming lectin in complex with sugars.
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J Biol Chem,
280,
17251-17259.
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PDB codes:
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M.J.Bernett,
T.Somasundaram,
and
M.Blaber
(2004).
An atomic resolution structure for human fibroblast growth factor 1.
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Proteins,
57,
626-634.
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PDB code:
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S.R.Brych,
J.Kim,
T.M.Logan,
and
M.Blaber
(2003).
Accommodation of a highly symmetric core within a symmetric protein superfold.
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Protein Sci,
12,
2704-2718.
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PDB codes:
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C.Liu,
J.A.Gaspar,
H.J.Wong,
and
E.M.Meiering
(2002).
Conserved and nonconserved features of the folding pathway of hisactophilin, a beta-trefoil protein.
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Protein Sci,
11,
669-679.
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R.S.Houliston,
C.Liu,
L.M.Singh,
and
E.M.Meiering
(2002).
pH and urea dependence of amide hydrogen-deuterium exchange rates in the beta-trefoil protein hisactophilin.
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Biochemistry,
41,
1182-1194.
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C.Liu,
D.Chu,
R.D.Wideman,
R.S.Houliston,
H.J.Wong,
and
E.M.Meiering
(2001).
Thermodynamics of denaturation of hisactophilin, a beta-trefoil protein.
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Biochemistry,
40,
3817-3827.
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S.R.Brych,
S.I.Blaber,
T.M.Logan,
and
M.Blaber
(2001).
Structure and stability effects of mutations designed to increase the primary sequence symmetry within the core region of a beta-trefoil.
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Protein Sci,
10,
2587-2599.
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PDB codes:
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Y.Lin,
R.A.Pixley,
and
R.W.Colman
(2000).
Kinetic analysis of the role of zinc in the interaction of domain 5 of high-molecular weight kininogen (HK) with heparin.
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Biochemistry,
39,
5104-5110.
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Y.Liu,
A.J.Chirino,
Z.Misulovin,
C.Leteux,
T.Feizi,
M.C.Nussenzweig,
and
P.J.Bjorkman
(2000).
Crystal structure of the cysteine-rich domain of mannose receptor complexed with a sulfated carbohydrate ligand.
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J Exp Med,
191,
1105-1116.
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PDB codes:
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F.Vallée,
A.Kadziola,
Y.Bourne,
M.Juy,
K.W.Rodenburg,
B.Svensson,
and
R.Haser
(1998).
Barley alpha-amylase bound to its endogenous protein inhibitor BASI: crystal structure of the complex at 1.9 A resolution.
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Structure,
6,
649-659.
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PDB code:
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T.R.Transue,
A.K.Smith,
H.Mo,
I.J.Goldstein,
and
M.A.Saper
(1997).
Structure of benzyl T-antigen disaccharide bound to Amaranthus caudatus agglutinin.
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Nat Struct Biol,
4,
779-783.
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PDB codes:
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C.Naumann,
C.Dietrich,
A.Behrisch,
T.Bayerl,
M.Schleicher,
D.Bucknall,
and
E.Sackmann
(1996).
Hisactophilin-mediated binding of actin to lipid lamellae: a neutron reflectivity study of protein membrane coupling.
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Biophys J,
71,
811-823.
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F.Hanakam,
R.Albrecht,
C.Eckerskorn,
M.Matzner,
and
G.Gerisch
(1996).
Myristoylated and non-myristoylated forms of the pH sensor protein hisactophilin II: intracellular shuttling to plasma membrane and nucleus monitored in real time by a fusion with green fluorescent protein.
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EMBO J,
15,
2935-2943.
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A.A.Noegel,
and
J.E.Luna
(1995).
The Dictyostelium cytoskeleton.
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Experientia,
51,
1135-1143.
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F.Hanakam,
C.Eckerskorn,
F.Lottspeich,
A.Müller-Taubenberger,
W.Schäfer,
and
G.Gerish
(1995).
The pH-sensitive actin-binding protein hisactophilin of Dictyostelium exists in two isoforms which both are myristoylated and distributed between plasma membrane and cytoplasm.
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J Biol Chem,
270,
596-602.
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H.A.Schreuder,
J.M.Rondeau,
C.Tardif,
A.Soffientini,
E.Sarubbi,
A.Akeson,
T.L.Bowlin,
S.Yanofsky,
and
R.W.Barrett
(1995).
Refined crystal structure of the interleukin-1 receptor antagonist. Presence of a disulfide link and a cis-proline.
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Eur J Biochem,
227,
838-847.
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PDB code:
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H.Zhu,
K.Ramnarayan,
J.Anchin,
W.Y.Miao,
A.Sereno,
L.Millman,
J.Zheng,
V.N.Balaji,
and
M.E.Wolff
(1995).
Glu-96 of basic fibroblast growth factor is essential for high affinity receptor binding. Identification by structure-based site-directed mutagenesis.
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J Biol Chem,
270,
21869-21874.
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U.Kavita,
and
S.B.Mizel
(1995).
Differential sensitivity of interleukin-1 alpha and -beta precursor proteins to cleavage by calpain, a calcium-dependent protease.
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J Biol Chem,
270,
27758-27765.
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W.M.Siders,
and
S.B.Mizel
(1995).
Interleukin-1 beta secretion. A possible multistep process that is regulated in a cell type-specific manner.
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J Biol Chem,
270,
16258-16264.
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A.E.Eriksson,
L.S.Cousens,
and
B.W.Matthews
(1993).
Refinement of the structure of human basic fibroblast growth factor at 1.6 A resolution and analysis of presumed heparin binding sites by selenate substitution.
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Protein Sci,
2,
1274-1284.
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PDB codes:
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M.Czisch,
M.Schleicher,
S.Hörger,
W.Voelter,
and
T.A.Holak
(1993).
Conformation of thymosin beta 4 in water determined by NMR spectroscopy.
|
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Eur J Biochem,
218,
335-344.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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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.
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