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PDBsum entry 1wlh
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Structural protein
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PDB id
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1wlh
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Contents |
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* Residue conservation analysis
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PDB id:
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Structural protein
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Title:
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Molecular structure of the rod domain of dictyostelium filamin
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Structure:
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Gelation factor. Chain: a, b. Fragment: repeat 4,5,6 rod domain. Synonym: actin binding protein 120, abp-120, ddfilamin. Engineered: yes
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Source:
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Dictyostelium discoideum. Organism_taxid: 44689. Gene: abpc. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
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Biol. unit:
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Dimer (from
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Resolution:
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2.80Å
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R-factor:
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0.258
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R-free:
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0.263
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Authors:
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G.M.Popowicz,R.Mueller,A.A.Noegel,M.Schleicher,R.Huber,T.A.Holak
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Key ref:
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G.M.Popowicz
et al.
(2004).
Molecular structure of the rod domain of dictyostelium filamin.
J Mol Biol,
342,
1637-1646.
PubMed id:
DOI:
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Date:
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27-Jun-04
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Release date:
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05-Oct-04
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PROCHECK
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Headers
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References
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P13466
(GELA_DICDI) -
Gelation factor from Dictyostelium discoideum
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Seq:
Struc:
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857 a.a.
308 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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J Mol Biol
342:1637-1646
(2004)
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PubMed id:
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Molecular structure of the rod domain of dictyostelium filamin.
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G.M.Popowicz,
R.Müller,
A.A.Noegel,
M.Schleicher,
R.Huber,
T.A.Holak.
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ABSTRACT
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Dictyostelium discoideum filamin (ddFLN) is a two-chain F-actin crosslinking
protein with an N-terminal actin-binding domain and a rod domain constructed
from six tandem repeats of a 100 residue motif that has an immunoglobulin (Ig)
fold. We report the 2.8 A resolution crystal structure of a homodimer of rod
repeats 4, 5 and 6. The two chains are arranged in an antiparallel fashion and
form an elongated element, which is shortened, however, compared to a fully
extended, linear configuration because the long axis of each Ig domain is
arranged at an angle to the long axis of the rod. Same arrangement of repeats
should also be present in the rod domain of human FLNa, much longer than
Dictyostelium FLN, which forms an extended structure able to crosslink F-actin
chains over distances of more than 1000 A.
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Selected figure(s)
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Figure 2.
Figure 2. Interpreted electron density map of the border
region between repeats 4 and 5. Pro647 placed between two
b-strands connects repeats. Additionally, side-chains of Glu565
and Arg734 form a salt-bridge.
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Figure 4.
Figure 4. A homodimer model of the whole ddFLN protein.
Inter-repeat angles are taken from repeats 4 and 5. Rod domain
builds an extended chain interconnecting two actin-binding
domains.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2004,
342,
1637-1646)
copyright 2004.
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Figures were
selected
by an automated process.
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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.A.Kesner,
S.L.Milgram,
B.R.Temple,
and
N.V.Dokholyan
(2010).
Isoform divergence of the filamin family of proteins.
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Mol Biol Evol,
27,
283-295.
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N.Pinotsis,
P.Abrusci,
K.Djinović-Carugo,
and
M.Wilmanns
(2009).
Terminal assembly of sarcomeric filaments by intermolecular beta-sheet formation.
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Trends Biochem Sci,
34,
33-39.
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E.Bura,
D.K.Klimov,
and
V.Barsegov
(2008).
Analyzing forced unfolding of protein tandems by ordered variates, 2: dependent unfolding times.
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Biophys J,
94,
2516-2528.
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K.S.Kolahi,
and
M.R.Mofrad
(2008).
Molecular mechanics of filamin's rod domain.
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Biophys J,
94,
1075-1083.
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N.Pinotsis,
S.Lange,
J.C.Perriard,
D.I.Svergun,
and
M.Wilmanns
(2008).
Molecular basis of the C-terminal tail-to-tail assembly of the sarcomeric filament protein myomesin.
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EMBO J,
27,
253-264.
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PDB code:
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E.Bura,
D.K.Klimov,
and
V.Barsegov
(2007).
Analyzing forced unfolding of protein tandems by ordered variates, 1: Independent unfolding times.
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Biophys J,
93,
1100-1115.
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F.Nakamura,
T.M.Osborn,
C.A.Hartemink,
J.H.Hartwig,
and
T.P.Stossel
(2007).
Structural basis of filamin A functions.
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J Cell Biol,
179,
1011-1025.
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S.J.Annesley,
E.Bandala-Sanchez,
A.U.Ahmed,
and
P.R.Fisher
(2007).
Filamin repeat segments required for photosensory signalling in Dictyostelium discoideum.
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BMC Cell Biol,
8,
48.
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Y.Lad,
T.Kiema,
P.Jiang,
O.T.Pentikäinen,
C.H.Coles,
I.D.Campbell,
D.A.Calderwood,
and
J.Ylänne
(2007).
Structure of three tandem filamin domains reveals auto-inhibition of ligand binding.
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EMBO J,
26,
3993-4004.
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PDB code:
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B.Wagner,
R.Tharmann,
I.Haase,
M.Fischer,
and
A.R.Bausch
(2006).
Cytoskeletal polymer networks: the molecular structure of cross-linkers determines macroscopic properties.
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Proc Natl Acad Sci U S A,
103,
13974-13978.
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G.M.Popowicz,
M.Schleicher,
A.A.Noegel,
and
T.A.Holak
(2006).
Filamins: promiscuous organizers of the cytoskeleton.
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Trends Biochem Sci,
31,
411-419.
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H.Dietz,
and
M.Rief
(2006).
Protein structure by mechanical triangulation.
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Proc Natl Acad Sci U S A,
103,
1244-1247.
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T.Kiema,
Y.Lad,
P.Jiang,
C.L.Oxley,
M.Baldassarre,
K.L.Wegener,
I.D.Campbell,
J.Ylänne,
and
D.A.Calderwood
(2006).
The molecular basis of filamin binding to integrins and competition with talin.
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Mol Cell,
21,
337-347.
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PDB code:
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E.Y.Levanon,
M.Hallegger,
Y.Kinar,
R.Shemesh,
K.Djinovic-Carugo,
G.Rechavi,
M.F.Jantsch,
and
E.Eisenberg
(2005).
Evolutionarily conserved human targets of adenosine to inosine RNA editing.
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Nucleic Acids Res,
33,
1162-1168.
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R.Pudas,
T.R.Kiema,
P.J.Butler,
M.Stewart,
and
J.Ylänne
(2005).
Structural basis for vertebrate filamin dimerization.
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Structure,
13,
111-119.
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PDB code:
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S.P.Robertson
(2005).
Filamin A: phenotypic diversity.
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Curr Opin Genet Dev,
15,
301-307.
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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
