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PDBsum entry 1acf
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Contractile protein
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PDB id
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1acf
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Contents |
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* Residue conservation analysis
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DOI no:
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Proc Natl Acad Sci U S A
91:8636-8640
(1994)
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PubMed id:
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X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates.
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A.A.Fedorov,
K.A.Magnus,
M.H.Graupe,
E.E.Lattman,
T.D.Pollard,
S.C.Almo.
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ABSTRACT
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We determined the structures of Acanthamoeba profilin I and profilin II by x-ray
crystallography at resolutions of 2.0 and 2.8 A, respectively. The polypeptide
folds and the actin-binding surfaces of the amoeba profilins are very similar to
those of bovine and human profilins. The electrostatic potential surfaces of the
two Acanthamoeba isoforms differ. Two areas of high positive potential on the
surface of profilin II are candidate binding sites for phosphatidylinositol
phosphates. The proximity of these sites to the actin binding site provides an
explanation for the competition between actin and lipids for binding profilin.
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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.Behnen,
K.Murk,
P.Kursula,
H.Cappallo-Obermann,
M.Rothkegel,
A.L.Kierszenbaum,
and
C.Kirchhoff
(2009).
Testis-expressed profilins 3 and 4 show distinct functional characteristics and localize in the acroplaxome-manchette complex in spermatids.
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BMC Cell Biol,
10,
34.
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R.Kardos,
K.Pozsonyi,
E.Nevalainen,
P.Lappalainen,
M.Nyitrai,
and
G.Hild
(2009).
The effects of ADF/cofilin and profilin on the conformation of the ATP-binding cleft of monomeric actin.
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Biophys J,
96,
2335-2343.
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T.Haikarainen,
W.Q.Chen,
G.Lubec,
and
P.Kursula
(2009).
Structure, modifications and ligand-binding properties of rat profilin 2a.
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Acta Crystallogr D Biol Crystallogr,
65,
303-311.
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PDB code:
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S.Morales,
J.C.Jiménez-López,
A.J.Castro,
M.I.Rodríguez-García,
and
J.D.Alché
(2008).
Olive pollen profilin (Ole e 2 allergen) co-localizes with highly active areas of the actin cytoskeleton and is released to the culture medium during in vitro pollen germination.
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J Microsc,
231,
332-341.
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A.J.Bojarski,
M.Nowak,
and
B.Testa
(2006).
Conformational fluctuations versus constraints in amino acid side chains: the evolution of information content from free amino acids to proteins.
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Chem Biodivers,
3,
245-273.
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D.Polet,
A.Lambrechts,
K.Ono,
A.Mah,
F.Peelman,
J.Vandekerckhove,
D.L.Baillie,
C.Ampe,
and
S.Ono
(2006).
Caenorhabditis elegans expresses three functional profilins in a tissue-specific manner.
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Cell Motil Cytoskeleton,
63,
14-28.
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L.J.Ball,
R.Kühne,
J.Schneider-Mergener,
and
H.Oschkinat
(2005).
Recognition of Proline-Rich Motifs by Protein-Protein-Interaction Domains.
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Angew Chem Int Ed Engl,
44,
2852-2869.
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W.Witke
(2004).
The role of profilin complexes in cell motility and other cellular processes.
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Trends Cell Biol,
14,
461-469.
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A.Lambrechts,
V.Jonckheere,
D.Dewitte,
J.Vandekerckhove,
and
C.Ampe
(2002).
Mutational analysis of human profilin I reveals a second PI(4,5)-P2 binding site neighbouring the poly(L-proline) binding site.
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BMC Biochem,
3,
12.
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J.Lu,
and
T.D.Pollard
(2001).
Profilin binding to poly-L-proline and actin monomers along with ability to catalyze actin nucleotide exchange is required for viability of fission yeast.
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Mol Biol Cell,
12,
1161-1175.
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M.Van Troys,
D.Dewitte,
J.L.Verschelde,
M.Goethals,
J.Vandekerckhove,
and
C.Ampe
(2000).
The competitive interaction of actin and PIP2 with actophorin is based on overlapping target sites: design of a gain-of-function mutant.
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Biochemistry,
39,
12181-12189.
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M.Van Troys,
J.Vandekerckhove,
and
C.Ampe
(1999).
Structural modules in actin-binding proteins: towards a new classification.
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Biochim Biophys Acta,
1448,
323-348.
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D.D.Billadeau,
K.M.Brumbaugh,
C.J.Dick,
R.A.Schoon,
X.R.Bustelo,
and
P.J.Leibson
(1998).
The Vav-Rac1 pathway in cytotoxic lymphocytes regulates the generation of cell-mediated killing.
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J Exp Med,
188,
549-559.
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J.C.Eads,
N.M.Mahoney,
S.Vorobiev,
A.R.Bresnick,
K.K.Wen,
P.A.Rubenstein,
B.K.Haarer,
and
S.C.Almo
(1998).
Structure determination and characterization of Saccharomyces cerevisiae profilin.
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Biochemistry,
37,
11171-11181.
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PDB code:
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V.K.Vinson,
E.M.De La Cruz,
H.N.Higgs,
and
T.D.Pollard
(1998).
Interactions of Acanthamoeba profilin with actin and nucleotides bound to actin.
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Biochemistry,
37,
10871-10880.
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Y.A.Puius,
N.M.Mahoney,
and
S.C.Almo
(1998).
The modular structure of actin-regulatory proteins.
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Curr Opin Cell Biol,
10,
23-34.
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A.A.Fedorov,
P.Lappalainen,
E.V.Fedorov,
D.G.Drubin,
and
S.C.Almo
(1997).
Structure determination of yeast cofilin.
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Nat Struct Biol,
4,
366-369.
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PDB codes:
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A.A.Fedorov,
T.Ball,
N.M.Mahoney,
R.Valenta,
and
S.C.Almo
(1997).
The molecular basis for allergen cross-reactivity: crystal structure and IgE-epitope mapping of birch pollen profilin.
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Structure,
5,
33-45.
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PDB code:
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J.A.Asturias,
M.C.Arilla,
B.Bartolomé,
J.Martínez,
A.Martínez,
and
R.Palacios
(1997).
Sequence polymorphism and structural analysis of timothy grass pollen profilin allergen (Phl p 11).
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Biochim Biophys Acta,
1352,
253-257.
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K.Djinovic Carugo,
S.Bañuelos,
and
M.Saraste
(1997).
Crystal structure of a calponin homology domain.
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Nat Struct Biol,
4,
175-179.
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PDB code:
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K.S.Thorn,
H.E.Christensen,
R.Shigeta,
D.Huddler,
L.Shalaby,
U.Lindberg,
N.H.Chua,
and
C.E.Schutt
(1997).
The crystal structure of a major allergen from plants.
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Structure,
5,
19-32.
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PDB codes:
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K.Schlüter,
B.M.Jockusch,
and
M.Rothkegel
(1997).
Profilins as regulators of actin dynamics.
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Biochim Biophys Acta,
1359,
97.
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L.A.Flanagan,
C.C.Cunningham,
J.Chen,
G.D.Prestwich,
K.S.Kosik,
and
P.A.Janmey
(1997).
The structure of divalent cation-induced aggregates of PIP2 and their alteration by gelsolin and tau.
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Biophys J,
73,
1440-1447.
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L.Vidali,
and
P.K.Hepler
(1997).
Characterization and localization of profilin in pollen grains and tubes of Lilium longiflorum.
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Cell Motil Cytoskeleton,
36,
323-338.
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E.C.Petrella,
L.M.Machesky,
D.A.Kaiser,
and
T.D.Pollard
(1996).
Structural requirements and thermodynamics of the interaction of proline peptides with profilin.
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Biochemistry,
35,
16535-16543.
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I.Karakesisoglou,
M.Schleicher,
B.C.Gibbon,
and
C.J.Staiger
(1996).
Plant profilins rescue the aberrant phenotype of profilin-deficient Dictyostelium cells.
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Cell Motil Cytoskeleton,
34,
36-47.
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M.K.Balasubramanian,
A.Feoktistova,
D.McCollum,
and
K.L.Gould
(1996).
Fission yeast Sop2p: a novel and evolutionarily conserved protein that interacts with Arp3p and modulates profilin function.
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EMBO J,
15,
6426-6437.
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P.J.Lu,
W.R.Shieh,
S.G.Rhee,
H.L.Yin,
and
C.S.Chen
(1996).
Lipid products of phosphoinositide 3-kinase bind human profilin with high affinity.
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Biochemistry,
35,
14027-14034.
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A.Lambrechts,
J.van Damme,
M.Goethals,
J.Vandekerckhove,
and
C.Ampe
(1995).
Purification and characterization of bovine profilin II. Actin, poly(L-proline) and inositolphospholipid binding.
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Eur J Biochem,
230,
281-286.
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R.Gieselmann,
D.J.Kwiatkowski,
P.A.Janmey,
and
W.Witke
(1995).
Distinct biochemical characteristics of the two human profilin isoforms.
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Eur J Biochem,
229,
621-628.
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W.J.Metzler,
B.T.Farmer,
K.L.Constantine,
M.S.Friedrichs,
T.Lavoie,
and
L.Mueller
(1995).
Refined solution structure of human profilin I.
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Protein Sci,
4,
450-459.
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PDB code:
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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
code is
shown on the right.
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Links
