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Protein fibril regulator
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PDB id
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2z6e
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Contents |
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* Residue conservation analysis
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PDB id:
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Protein fibril regulator
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Title:
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Crystal structure of human daam1 fh2
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Structure:
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Disheveled-associated activator of morphogenesis 1. Chain: a, b, c, d. Fragment: fh2 domain, unp residues 594-1012. Synonym: formin. Engineered: yes
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Source:
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Homo sapiens. Human. Gene: daam1. Expressed in: escherichia coli.
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Resolution:
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2.80Å
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R-factor:
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0.225
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R-free:
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0.289
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Authors:
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M.Yamashita,T.Higashi,Y.Sato,R.Shirakawa,T.Kita,H.Horiuchi, S.Fukai,O.Nureki
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Key ref:
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M.Yamashita
et al.
(2007).
Crystal structure of human DAAM1 formin homology 2 domain.
Genes Cells,
12,
1255-1265.
PubMed id:
DOI:
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Date:
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31-Jul-07
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Release date:
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27-May-08
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PROCHECK
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Headers
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References
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Q9Y4D1
(DAAM1_HUMAN) -
Disheveled-associated activator of morphogenesis 1
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Seq:
Struc:
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1078 a.a.
388 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Gene Ontology (GO) functional annotation
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Biological process
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cellular component organization
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2 terms
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Biochemical function
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actin binding
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1 term
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DOI no:
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Genes Cells
12:1255-1265
(2007)
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PubMed id:
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Crystal structure of human DAAM1 formin homology 2 domain.
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M.Yamashita,
T.Higashi,
S.Suetsugu,
Y.Sato,
T.Ikeda,
R.Shirakawa,
T.Kita,
T.Takenawa,
H.Horiuchi,
S.Fukai,
O.Nureki.
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ABSTRACT
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Reorganization of the actin filament is an essential process for cell motility,
cell-cell attachment and intracellular transport. Formin proteins promote
nucleation and elongation of the actin filament, and thus are key regulators for
this process. The formin homology 2 (FH2) domain forms a head-to-tail
ring-shaped dimer, and processively moves towards the barbed end.
Dishevelled-associated activator of morphogenesis (DAAM) is a Rho-regulated
formin implicated in neuronal development. Here, we present the crystal
structure of human DAAM1 FH2 dimer at 2.8 A resolution. This is the first
dimeric structure of the mammalian formin. The core structure of human DAAM1 is
similar to those of mouse mDia1 and yeast Bni1p, whereas the orientations of the
FH2 dimeric rings are different between human DAAM1 and yeast Bni1p, despite
their similar dimer interactions. This difference supports the previous
prediction that the dimer architecture of the formin is highly flexible in the
actin-free state. The results of the actin assembly assays using the DAAM1
mutants demonstrated that the length of the linker connecting the N-terminal
domain and the core region is crucial for the activity.
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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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A.Nezami,
F.Poy,
A.Toms,
W.Zheng,
and
M.J.Eck
(2010).
Crystal structure of a complex between amino and carboxy terminal fragments of mDia1: insights into autoinhibition of diaphanous-related formins.
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PLoS One, 5,
0.
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PDB code:
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M.A.Chesarone,
A.G.DuPage,
and
B.L.Goode
(2010).
Unleashing formins to remodel the actin and microtubule cytoskeletons.
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Nat Rev Mol Cell Biol, 11,
62-74.
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R.Liu,
E.V.Linardopoulou,
G.E.Osborn,
and
S.M.Parkhurst
(2010).
Formins in development: orchestrating body plan origami.
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Biochim Biophys Acta, 1803,
207-225.
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S.Barkó,
B.Bugyi,
M.F.Carlier,
R.Gombos,
T.Matusek,
J.Mihály,
and
M.Nyitrai
(2010).
Characterization of the biochemical properties and biological function of the formin homology domains of Drosophila DAAM.
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J Biol Chem, 285,
13154-13169.
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S.F.Ang,
Z.S.Zhao,
L.Lim,
and
E.Manser
(2010).
DAAM1 is a formin required for centrosome re-orientation during cell migration.
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PLoS One, 5,
0.
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T.Higashi,
T.Ikeda,
T.Murakami,
R.Shirakawa,
M.Kawato,
K.Okawa,
M.Furuse,
T.Kimura,
T.Kita,
and
H.Horiuchi
(2010).
Flightless-I (Fli-I) regulates the actin assembly activity of diaphanous-related formins (DRFs) Daam1 and mDia1 in cooperation with active Rho GTPase.
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J Biol Chem, 285,
16231-16238.
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A.S.Paul,
and
T.D.Pollard
(2009).
Energetic requirements for processive elongation of actin filaments by FH1FH2-formins.
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J Biol Chem, 284,
12533-12540.
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D.K.Khadka,
W.Liu,
and
R.Habas
(2009).
Non-redundant roles for Profilin2 and Profilin1 during vertebrate gastrulation.
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Dev Biol, 332,
396-406.
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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
