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PDBsum entry 1ux5
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Structural protein
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PDB id
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1ux5
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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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Crystal structures of a formin homology-2 domain reveal a flexibly tethered dimer architecture
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Structure:
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Bni1 protein. Chain: a. Fragment: fh2 domain, residues 1350-1760. Synonym: formin, synthetic lethal 39. Engineered: yes
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Source:
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Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Expressed in: escherichia coli. Expression_system_taxid: 562
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Biol. unit:
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Dimer (from PDB file)
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Resolution:
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2.50Å
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R-factor:
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0.207
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R-free:
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0.251
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Authors:
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Y.Xu,J.B.Moseley,I.Sagot,F.Poy,D.Pellman,B.L.Goode,M.J.Eck
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Key ref:
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Y.Xu
et al.
(2004).
Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture.
Cell,
116,
711-723.
PubMed id:
DOI:
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Date:
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19-Feb-04
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Release date:
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11-Mar-04
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PROCHECK
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Headers
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References
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P41832
(BNI1_YEAST) -
Protein BNI1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq: Struc:
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1953 a.a.
411 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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DOI no:
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Cell
116:711-723
(2004)
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PubMed id:
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Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture.
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Y.Xu,
J.B.Moseley,
I.Sagot,
F.Poy,
D.Pellman,
B.L.Goode,
M.J.Eck.
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ABSTRACT
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Formin proteins participate in a wide range of cytoskeletal processes in all
eukaryotes. The defining feature of formins is a highly conserved approximately
400 residue region, the Formin Homology-2 (FH2) domain, which has recently been
found to nucleate actin filaments. Here we report crystal structures of the S.
cerevesiae Bni1p FH2 domain. The mostly alpha-helical FH2 domain forms a unique
"tethered dimer" in which two elongated actin binding heads are tied
together at either end by an unusual lasso and linker structure. Biochemical and
crystallographic observations indicate that the dimer is stable but flexible,
with flexibility between the two halves of the dimer conferred by the linker
segments. Although each half of the dimer is competent to interact with filament
ends, the intact dimer is required for actin nucleation and processive capping.
The tethered dimer architecture may allow formins to stair-step on the barbed
end of an elongating nascent filament.
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Selected figure(s)
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Figure 1.
Figure 1. Three-Dimensional Structure of the
FH2 Domain Dimmer
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Figure 7.
Figure 7. A Speculative Model Showing How the Tethered Dimer Architecture of the FH2 Domain Could Allow Stair-Stepping on the Elongating
Barbed End of F-Actin
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2004,
116,
711-723)
copyright 2004.
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Figures were
selected
by the author.
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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.E.Thompson,
E.G.Heimsath,
T.J.Gauvin,
H.N.Higgs,
and
F.J.Kull
(2013).
FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation.
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Nat Struct Mol Biol,
20,
111-118.
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PDB code:
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B.Yu,
H.C.Cheng,
C.A.Brautigam,
D.R.Tomchick,
and
M.K.Rosen
(2011).
Mechanism of actin filament nucleation by the bacterial effector VopL.
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Nat Struct Mol Biol,
18,
1068-1074.
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PDB code:
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E.Karaca,
and
A.M.Bonvin
(2011).
A multidomain flexible docking approach to deal with large conformational changes in the modeling of biomolecular complexes.
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Structure,
19,
555-565.
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P.O.Widlund,
J.H.Stear,
A.Pozniakovsky,
M.Zanic,
S.Reber,
G.J.Brouhard,
A.A.Hyman,
and
J.Howard
(2011).
XMAP215 polymerase activity is built by combining multiple tubulin-binding TOG domains and a basic lattice-binding region.
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Proc Natl Acad Sci U S A,
108,
2741-2746.
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R.Dominguez,
and
K.C.Holmes
(2011).
Actin structure and function.
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Annu Rev Biophys,
40,
169-186.
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X.H.Xue,
C.Q.Guo,
F.Du,
Q.L.Lu,
C.M.Zhang,
and
H.Y.Ren
(2011).
AtFH8 is involved in root development under effect of low-dose latrunculin B in dividing cells.
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Mol Plant,
4,
264-278.
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A.M.Ducka,
P.Joel,
G.M.Popowicz,
K.M.Trybus,
M.Schleicher,
A.A.Noegel,
R.Huber,
T.A.Holak,
and
T.Sitar
(2010).
Structures of actin-bound Wiskott-Aldrich syndrome protein homology 2 (WH2) domains of Spire and the implication for filament nucleation.
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Proc Natl Acad Sci U S A,
107,
11757-11762.
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PDB codes:
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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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A.Yonetani,
and
F.Chang
(2010).
Regulation of cytokinesis by the formin cdc12p.
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Curr Biol,
20,
561-566.
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E.S.Harris,
T.J.Gauvin,
E.G.Heimsath,
and
H.N.Higgs
(2010).
Assembly of filopodia by the formin FRL2 (FMNL3).
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Cytoskeleton (Hoboken),
67,
755-772.
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H.G.Mannherz,
A.J.Mazur,
and
B.Jockusch
(2010).
Repolymerization of actin from actin:thymosin beta4 complex induced by diaphanous related formins and gelsolin.
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Ann N Y Acad Sci,
1194,
36-43.
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H.I.Balcer,
K.Daugherty-Clarke,
and
B.L.Goode
(2010).
The p40/ARPC1 subunit of Arp2/3 complex performs multiple essential roles in WASp-regulated actin nucleation.
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J Biol Chem,
285,
8481-8491.
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K.G.Campellone,
and
M.D.Welch
(2010).
A nucleator arms race: cellular control of actin assembly.
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Nat Rev Mol Cell Biol,
11,
237-251.
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L.Andrés-Delgado,
O.M.Antón,
R.Madrid,
J.A.Byrne,
and
M.A.Alonso
(2010).
Formin INF2 regulates MAL-mediated transport of Lck to the plasma membrane of human T lymphocytes.
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Blood,
116,
5919-5929.
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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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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.H.Lee,
and
R.Dominguez
(2010).
Regulation of actin cytoskeleton dynamics in cells.
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Mol Cells,
29,
311-325.
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T.Iskratsch,
S.Lange,
J.Dwyer,
A.L.Kho,
C.dos Remedios,
and
E.Ehler
(2010).
Formin follows function: a muscle-specific isoform of FHOD3 is regulated by CK2 phosphorylation and promotes myofibril maintenance.
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J Cell Biol,
191,
1159-1172.
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T.Otomo,
D.R.Tomchick,
C.Otomo,
M.Machius,
and
M.K.Rosen
(2010).
Crystal structure of the Formin mDia1 in autoinhibited conformation.
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PLoS One,
5,
0.
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PDB code:
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W.Daher,
F.Plattner,
M.F.Carlier,
and
D.Soldati-Favre
(2010).
Concerted action of two formins in gliding motility and host cell invasion by Toxoplasma gondii.
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PLoS Pathog,
6,
0.
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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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A.S.Paul,
and
T.D.Pollard
(2009).
Review of the mechanism of processive actin filament elongation by formins.
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Cell Motil Cytoskeleton,
66,
606-617.
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D.Kumar,
and
A.B.Lassar
(2009).
The transcriptional activity of Sox9 in chondrocytes is regulated by RhoA signaling and actin polymerization.
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Mol Cell Biol,
29,
4262-4273.
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K.K.Wen,
and
P.A.Rubenstein
(2009).
Differential regulation of actin polymerization and structure by yeast formin isoforms.
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J Biol Chem,
284,
16776-16783.
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K.Taniguchi,
R.Takeya,
S.Suetsugu,
M.Kan-O,
M.Narusawa,
A.Shiose,
R.Tominaga,
and
H.Sumimoto
(2009).
Mammalian formin fhod3 regulates actin assembly and sarcomere organization in striated muscles.
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J Biol Chem,
284,
29873-29881.
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T.J.Gauvin,
J.Fukui,
J.R.Peterson,
and
H.N.Higgs
(2009).
Isoform-selective chemical inhibition of mDia-mediated actin assembly.
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Biochemistry,
48,
9327-9329.
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A.S.Paul,
A.Paul,
T.D.Pollard,
and
T.Pollard
(2008).
The role of the FH1 domain and profilin in formin-mediated actin-filament elongation and nucleation.
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Curr Biol,
18,
9.
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A.Schulte,
B.Stolp,
A.Schönichen,
O.Pylypenko,
A.Rak,
O.T.Fackler,
and
M.Geyer
(2008).
The human formin FHOD1 contains a bipartite structure of FH3 and GTPase-binding domains required for activation.
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Structure,
16,
1313-1323.
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PDB code:
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A.Yonetani,
R.J.Lustig,
J.B.Moseley,
T.Takeda,
B.L.Goode,
and
F.Chang
(2008).
Regulation and targeting of the fission yeast formin cdc12p in cytokinesis.
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Mol Biol Cell,
19,
2208-2219.
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C.Baarlink,
and
R.Grosse
(2008).
A GBD uncovered: the FHOD1 N terminus is formin'.
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Structure,
16,
1287-1288.
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D.Chalkia,
N.Nikolaidis,
W.Makalowski,
J.Klein,
and
M.Nei
(2008).
Origins and evolution of the formin multigene family that is involved in the formation of actin filaments.
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Mol Biol Evol,
25,
2717-2733.
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E.M.Neidt,
C.T.Skau,
and
D.R.Kovar
(2008).
The cytokinesis formins from the nematode worm and fission yeast differentially mediate actin filament assembly.
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J Biol Chem,
283,
23872-23883.
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F.Bartolini,
J.B.Moseley,
J.Schmoranzer,
L.Cassimeris,
B.L.Goode,
and
G.G.Gundersen
(2008).
The formin mDia2 stabilizes microtubules independently of its actin nucleation activity.
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J Cell Biol,
181,
523-536.
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H.Wang,
and
D.Vavylonis
(2008).
Model of For3p-mediated actin cable assembly in fission yeast.
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PLoS ONE,
3,
e4078.
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J.Baum,
C.J.Tonkin,
A.S.Paul,
M.Rug,
B.J.Smith,
S.B.Gould,
D.Richard,
T.D.Pollard,
and
A.F.Cowman
(2008).
A malaria parasite formin regulates actin polymerization and localizes to the parasite-erythrocyte moving junction during invasion.
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Cell Host Microbe,
3,
188-198.
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M.Dettenhofer,
F.Zhou,
and
P.Leder
(2008).
Formin 1-isoform IV deficient cells exhibit defects in cell spreading and focal adhesion formation.
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PLoS ONE,
3,
e2497.
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M.Lammers,
S.Meyer,
D.Kühlmann,
and
A.Wittinghofer
(2008).
Specificity of Interactions between mDia Isoforms and Rho Proteins.
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J Biol Chem,
283,
35236-35246.
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PDB code:
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N.A.Gloushankova
(2008).
Changes in regulation of cell-cell adhesion during tumor transformation.
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Biochemistry (Mosc),
73,
742-750.
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S.Watanabe,
Y.Ando,
S.Yasuda,
H.Hosoya,
N.Watanabe,
T.Ishizaki,
and
S.Narumiya
(2008).
mDia2 induces the actin scaffold for the contractile ring and stabilizes its position during cytokinesis in NIH 3T3 cells.
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Mol Biol Cell,
19,
2328-2338.
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T.Higashi,
T.Ikeda,
R.Shirakawa,
H.Kondo,
M.Kawato,
M.Horiguchi,
T.Okuda,
K.Okawa,
S.Fukai,
O.Nureki,
T.Kita,
and
H.Horiuchi
(2008).
Biochemical characterization of the Rho GTPase-regulated actin assembly by diaphanous-related formins, mDia1 and Daam1, in platelets.
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J Biol Chem,
283,
8746-8755.
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W.Liu,
A.Sato,
D.Khadka,
R.Bharti,
H.Diaz,
L.W.Runnels,
and
R.Habas
(2008).
Mechanism of activation of the Formin protein Daam1.
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Proc Natl Acad Sci U S A,
105,
210-215.
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B.L.Goode,
and
M.J.Eck
(2007).
Mechanism and function of formins in the control of actin assembly.
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Annu Rev Biochem,
76,
593-627.
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B.Wawro,
N.J.Greenfield,
M.A.Wear,
J.A.Cooper,
H.N.Higgs,
and
S.E.Hitchcock-DeGregori
(2007).
Tropomyosin regulates elongation by formin at the fast-growing end of the actin filament.
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Biochemistry,
46,
8146-8155.
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D.T.Brandt,
S.Marion,
G.Griffiths,
T.Watanabe,
K.Kaibuchi,
and
R.Grosse
(2007).
Dia1 and IQGAP1 interact in cell migration and phagocytic cup formation.
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J Cell Biol,
178,
193-200.
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H.O.Park,
and
E.Bi
(2007).
Central roles of small GTPases in the development of cell polarity in yeast and beyond.
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Microbiol Mol Biol Rev,
71,
48-96.
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J.Lu,
W.Meng,
F.Poy,
S.Maiti,
B.L.Goode,
and
M.J.Eck
(2007).
Structure of the FH2 domain of Daam1: implications for formin regulation of actin assembly.
|
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J Mol Biol,
369,
1258-1269.
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PDB code:
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M.E.Quinlan,
S.Hilgert,
A.Bedrossian,
R.D.Mullins,
and
E.Kerkhoff
(2007).
Regulatory interactions between two actin nucleators, Spire and Cappuccino.
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J Cell Biol,
179,
117-128.
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M.Yamashita,
T.Higashi,
S.Suetsugu,
Y.Sato,
T.Ikeda,
R.Shirakawa,
T.Kita,
T.Takenawa,
H.Horiuchi,
S.Fukai,
and
O.Nureki
(2007).
Crystal structure of human DAAM1 formin homology 2 domain.
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Genes Cells,
12,
1255-1265.
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PDB code:
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S.G.Martin,
S.A.Rincón,
R.Basu,
P.Pérez,
and
F.Chang
(2007).
Regulation of the formin for3p by cdc42p and bud6p.
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Mol Biol Cell,
18,
4155-4167.
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S.M.Buttery,
S.Yoshida,
and
D.Pellman
(2007).
Yeast formins Bni1 and Bnr1 utilize different modes of cortical interaction during the assembly of actin cables.
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Mol Biol Cell,
18,
1826-1838.
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T.D.Pollard
(2007).
Regulation of actin filament assembly by Arp2/3 complex and formins.
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Annu Rev Biophys Biomol Struct,
36,
451-477.
|
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T.M.Kitzing,
A.S.Sahadevan,
D.T.Brandt,
H.Knieling,
S.Hannemann,
O.T.Fackler,
J.Grosshans,
and
R.Grosse
(2007).
Positive feedback between Dia1, LARG, and RhoA regulates cell morphology and invasion.
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Genes Dev,
21,
1478-1483.
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A.Schönichen,
M.Alexander,
J.E.Gasteier,
F.E.Cuesta,
O.T.Fackler,
and
M.Geyer
(2006).
Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1.
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| |
J Biol Chem,
281,
5084-5093.
|
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A.Seth,
C.Otomo,
and
M.K.Rosen
(2006).
Autoinhibition regulates cellular localization and actin assembly activity of the diaphanous-related formins FRLalpha and mDia1.
|
| |
J Cell Biol,
174,
701-713.
|
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B.Bugyi,
G.Papp,
G.Hild,
D.Lõrinczy,
E.M.Nevalainen,
P.Lappalainen,
B.Somogyi,
and
M.Nyitrai
(2006).
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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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
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}
}
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