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Cell-division protein
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PDB id
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1fsz
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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Cellular component
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protein complex
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2 terms
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Biological process
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cell cycle
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4 terms
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Biochemical function
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nucleotide binding
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3 terms
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DOI no:
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Nature
391:203-206
(1998)
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PubMed id:
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Crystal structure of the bacterial cell-division protein FtsZ.
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J.Löwe,
L.A.Amos.
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ABSTRACT
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Bacterial cell division ends with septation, the constriction of the cell wall
and cell membranes that leads to the formation of two daughter cells. During
septation, FtsZ, a protein of relative molecular mass 40,000 which is ubiquitous
in eubacteria and is also found in archaea and chloroplasts, localizes early at
the division site to form a ring-shaped septum. This septum is required for the
mechanochemical process of membrane constriction. FtsZ is a GTPase with weak
sequence homology to tubulins. The nature of FtsZ polymers in vivo is unknown,
but FtsZ can form tubules, sheets and minirings in vitro. Here we report the
crystal structure at 2.8 A resolution of recombinant FtsZ from the
hyperthermophilic methanogen Methanococcus jannaschii. FtsZ has two domains, one
of which is a GTPase domain with a fold related to one found in the proteins
p21ras and elongation factor EF-Tu. The carboxy-terminal domain, whose function
is unknown, is a four-stranded beta-sheet tilted by 90 degrees against the
beta-sheet of the GTPase domain. The two domains are arranged around a central
helix. GDP binding is different from that typically found in GTPases and
involves four phosphate-binding loops and a sugar-binding loop in the first
domain, with guanine being recognized by residues in the central connecting
helix. The three-dimensional structure of FtsZ is similar to the structure of
alpha- and beta-tubulin.
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Selected figure(s)
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Figure 1.
Figure 1 Ribbon drawings of FtsZ (residues 23-356) from
M.jannaschii. a, View showing the GTPase domain in blue/green,
the C-terminal domain in red/orange, and the connecting helix H5
in yellow. GDP is represented by a space-filling model. b, View
of FtsZ rotated by  90°
from that in a. GDP is represented by a ball-and-stick model.
Figures were prepared with POVSCRIPT (D. Peisach, personal
communication)28.
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Figure 3.
Figure 3 Stereo plot of the active site of FtsZ. Superimposed
is the final 2F [0]-F [c] electron density map for the
nucleotide contoured at 1  .Prepared
with MOLSCRIPT28.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nature
(1998,
391,
203-206)
copyright 1998.
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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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C.Fraipont,
S.Alexeeva,
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M.Schloesser,
T.den Blaauwen,
and
M.Nguyen-Distèche
(2011).
The integral membrane FtsW protein and peptidoglycan synthase PBP3 form a subcomplex in Escherichia coli.
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| |
Microbiology, 157,
251-259.
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D.Awasthi,
K.Kumar,
and
I.Ojima
(2011).
Therapeutic potential of FtsZ inhibition: a patent perspective.
|
| |
Expert Opin Ther Pat, 21,
657-679.
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|
|
|
|
|
D.Popp,
and
R.C.Robinson
(2011).
Many ways to build an actin filament.
|
| |
Mol Microbiol, 80,
300-308.
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|
|
|
|
|
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D.W.Adams,
L.J.Wu,
L.G.Czaplewski,
and
J.Errington
(2011).
Multiple effects of benzamide antibiotics on FtsZ function.
|
| |
Mol Microbiol, 80,
68-84.
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|
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H.Cho,
H.R.McManus,
S.L.Dove,
and
T.G.Bernhardt
(2011).
Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist.
|
| |
Proc Natl Acad Sci U S A, 108,
3773-3778.
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|
|
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|
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K.Voigt,
and
P.M.Kirk
(2011).
Recent developments in the taxonomic affiliation and phylogenetic positioning of fungi: impact in applied microbiology and environmental biotechnology.
|
| |
Appl Microbiol Biotechnol, 90,
41-57.
|
|
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M.T.Cabeen,
H.Herrmann,
and
C.Jacobs-Wagner
(2011).
The domain organization of the bacterial intermediate filament-like protein crescentin is important for assembly and function.
|
| |
Cytoskeleton (Hoboken), 68,
205-219.
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|
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|
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|
|
D.J.Haydon,
J.M.Bennett,
D.Brown,
I.Collins,
G.Galbraith,
P.Lancett,
R.Macdonald,
N.R.Stokes,
P.K.Chauhan,
J.K.Sutariya,
N.Nayal,
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J.Beanland,
R.Hall,
V.Henstock,
C.Noula,
C.Rockley,
and
L.Czaplewski
(2010).
Creating an antibacterial with in vivo efficacy: synthesis and characterization of potent inhibitors of the bacterial cell division protein FtsZ with improved pharmaceutical properties.
|
| |
J Med Chem, 53,
3927-3936.
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E.I.Tocheva,
Z.Li,
and
G.J.Jensen
(2010).
Electron cryotomography.
|
| |
Cold Spring Harb Perspect Biol, 2,
a003442.
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E.Nogales
(2010).
When cytoskeletal worlds collide.
|
| |
Proc Natl Acad Sci U S A, 107,
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I.F.de Oliveira,
A.de Sousa Borges,
V.Kooij,
J.Bartosiak-Jentys,
J.Luirink,
and
D.J.Scheffers
(2010).
Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC.
|
| |
PLoS One, 5,
e12048.
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J.Hritz,
T.Läppchen,
and
C.Oostenbrink
(2010).
Calculations of binding affinity between C8-substituted GTP analogs and the bacterial cell-division protein FtsZ.
|
| |
Eur Biophys J, 39,
1573-1580.
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J.Strömqvist,
K.Skoog,
D.O.Daley,
J.Widengren,
and
G.von Heijne
(2010).
Estimating Z-ring radius and contraction in dividing Escherichia coli.
|
| |
Mol Microbiol, 76,
151-158.
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K.Ksiazek
(2010).
Bacterial aging: from mechanistic basis to evolutionary perspective.
|
| |
Cell Mol Life Sci, 67,
3131-3137.
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M.Ingerson-Mahar,
A.Briegel,
J.N.Werner,
G.J.Jensen,
and
Z.Gitai
(2010).
The metabolic enzyme CTP synthase forms cytoskeletal filaments.
|
| |
Nat Cell Biol, 12,
739-746.
|
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M.T.Cabeen,
and
C.Jacobs-Wagner
(2010).
A metabolic assembly line in bacteria.
|
| |
Nat Cell Biol, 12,
731-733.
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M.T.Cabeen,
and
C.Jacobs-Wagner
(2010).
The bacterial cytoskeleton.
|
| |
Annu Rev Genet, 44,
365-392.
|
|
|
|
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|
|
M.Thanbichler
(2010).
Synchronization of chromosome dynamics and cell division in bacteria.
|
| |
Cold Spring Harb Perspect Biol, 2,
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|
|
|
|
|
|
|
P.Gupta,
H.Rajeswari,
M.Arumugam,
S.Mishra,
R.Bhagavat,
P.Anand,
N.Chandra,
R.Srinivasan,
S.Indi,
and
P.Ajitkumar
(2010).
Mycobacterium tuberculosis FtsZ requires at least one arginine residue at the C-terminal end for polymerization in vitro.
|
| |
Acta Biochim Biophys Sin (Shanghai), 42,
58-69.
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|
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R.Bernander,
and
T.J.Ettema
(2010).
FtsZ-less cell division in archaea and bacteria.
|
| |
Curr Opin Microbiol, 13,
747-752.
|
|
|
|
|
|
|
R.V.Ulijn,
and
P.F.Caponi
(2010).
Bioinspired chemistry: rewiring nanostructures.
|
| |
Nat Chem, 2,
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|
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|
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A.J.Schmitz,
J.M.Glynn,
B.J.Olson,
K.D.Stokes,
and
K.W.Osteryoung
(2009).
Arabidopsis FtsZ2-1 and FtsZ2-2 Are Functionally Redundant, But FtsZ-Based Plastid Division Is Not Essential for Chloroplast Partitioning or Plant Growth and Development.
|
| |
Mol Plant, 2,
1211-1222.
|
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A.Martin,
D.Lang,
S.T.Hanke,
S.J.Mueller,
E.Sarnighausen,
M.Vervliet-Scheebaum,
and
R.Reski
(2009).
Targeted Gene Knockouts Reveal Overlapping Functions of the Five Physcomitrella patens FtsZ Isoforms in Chloroplast Division, Chloroplast Shaping, Cell Patterning, Plant Development, and Gravity Sensing.
|
| |
Mol Plant, 2,
1359-1372.
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|
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A.Niehl,
and
M.Heinlein
(2009).
Impact of RNA virus infection on plant cell function and evolution.
|
| |
Ann N Y Acad Sci, 1178,
120-128.
|
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|
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|
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A.Raymond,
S.Lovell,
D.Lorimer,
J.Walchli,
M.Mixon,
E.Wallace,
K.Thompkins,
K.Archer,
A.Burgin,
and
L.Stewart
(2009).
Combined protein construct and synthetic gene engineering for heterologous protein expression and crystallization using Gene Composer.
|
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BMC Biotechnol, 9,
37.
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PDB codes:
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B.Shen,
and
J.Lutkenhaus
(2009).
The conserved C-terminal tail of FtsZ is required for the septal localization and division inhibitory activity of MinC(C)/MinD.
|
| |
Mol Microbiol, 72,
410-424.
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D.W.Adams,
and
J.Errington
(2009).
Bacterial cell division: assembly, maintenance and disassembly of the Z ring.
|
| |
Nat Rev Microbiol, 7,
642-653.
|
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|
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E.Wilcox,
C.McGrath,
A.V.Blokhin,
R.Gussio,
and
E.Hamel
(2009).
Evidence for a distinct ligand binding site on tubulin discovered through inhibition by GDP of paclitaxel-induced tubulin assembly in the absence of exogenous GTP.
|
| |
Arch Biochem Biophys, 484,
55-62.
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I.Inoue,
R.Ino,
and
A.Nishimura
(2009).
New model for assembly dynamics of bacterial tubulin in relation to the stages of DNA replication.
|
| |
Genes Cells, 14,
435-444.
|
|
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|
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|
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J.Dworkin
(2009).
Cellular polarity in prokaryotic organisms.
|
| |
Cold Spring Harb Perspect Biol, 1,
a003368.
|
|
|
|
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|
|
M.Kudryashev,
M.Cyrklaff,
W.Baumeister,
M.M.Simon,
R.Wallich,
and
F.Frischknecht
(2009).
Comparative cryo-electron tomography of pathogenic Lyme disease spirochetes.
|
| |
Mol Microbiol, 71,
1415-1434.
|
|
|
|
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|
|
P.Gamba,
J.W.Veening,
N.J.Saunders,
L.W.Hamoen,
and
R.A.Daniel
(2009).
Two-step assembly dynamics of the Bacillus subtilis divisome.
|
| |
J Bacteriol, 191,
4186-4194.
|
|
|
|
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|
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P.L.Graumann
(2009).
Dynamics of bacterial cytoskeletal elements.
|
| |
Cell Motil Cytoskeleton, 66,
909-914.
|
|
|
|
|
|
|
Q.Xu,
B.A.Traag,
J.Willemse,
D.McMullan,
M.D.Miller,
M.A.Elsliger,
P.Abdubek,
T.Astakhova,
H.L.Axelrod,
C.Bakolitsa,
D.Carlton,
C.Chen,
H.J.Chiu,
M.Chruszcz,
T.Clayton,
D.Das,
M.C.Deller,
L.Duan,
K.Ellrott,
D.Ernst,
C.L.Farr,
J.Feuerhelm,
J.C.Grant,
A.Grzechnik,
S.K.Grzechnik,
G.W.Han,
L.Jaroszewski,
K.K.Jin,
H.E.Klock,
M.W.Knuth,
P.Kozbial,
S.S.Krishna,
A.Kumar,
D.Marciano,
W.Minor,
A.M.Mommaas,
A.T.Morse,
E.Nigoghossian,
A.Nopakun,
L.Okach,
S.Oommachen,
J.Paulsen,
C.Puckett,
R.Reyes,
C.L.Rife,
N.Sefcovic,
H.J.Tien,
C.B.Trame,
H.van den Bedem,
S.Wang,
D.Weekes,
K.O.Hodgson,
J.Wooley,
A.M.Deacon,
A.Godzik,
S.A.Lesley,
I.A.Wilson,
and
G.P.van Wezel
(2009).
Structural and functional characterizations of SsgB, a conserved activator of developmental cell division in morphologically complex actinomycetes.
|
| |
J Biol Chem, 284,
25268-25279.
|
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PDB code:
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R.H.Wade
(2009).
On and around microtubules: an overview.
|
| |
Mol Biotechnol, 43,
177-191.
|
|
|
|
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|
|
R.Reski
(2009).
Challenges to our current view on chloroplasts.
|
| |
Biol Chem, 390,
731-738.
|
|
|
|
|
|
|
T.K.Beuria,
P.Singh,
A.Surolia,
and
D.Panda
(2009).
Promoting assembly and bundling of FtsZ as a strategy to inhibit bacterial cell division: a new approach for developing novel antibacterial drugs.
|
| |
Biochem J, 423,
61-69.
|
|
|
|
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|
|
V.Norris,
and
R.Root-Bernstein
(2009).
The eukaryotic cell originated in the integration and redistribution of hyperstructures from communities of prokaryotic cells based on molecular complementarity.
|
| |
Int J Mol Sci, 10,
2611-2632.
|
|
|
|
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|
|
W.Margolin
(2009).
Sculpting the bacterial cell.
|
| |
Curr Biol, 19,
R812-R822.
|
|
|
|
|
|
|
D.Claessen,
R.Emmins,
L.W.Hamoen,
R.A.Daniel,
J.Errington,
and
D.H.Edwards
(2008).
Control of the cell elongation-division cycle by shuttling of PBP1 protein in Bacillus subtilis.
|
| |
Mol Microbiol, 68,
1029-1046.
|
|
|
|
|
|
|
D.J.Haydon,
N.R.Stokes,
R.Ure,
G.Galbraith,
J.M.Bennett,
D.R.Brown,
P.J.Baker,
V.V.Barynin,
D.W.Rice,
S.E.Sedelnikova,
J.R.Heal,
J.M.Sheridan,
S.T.Aiwale,
P.K.Chauhan,
A.Srivastava,
A.Taneja,
I.Collins,
J.Errington,
and
L.G.Czaplewski
(2008).
An inhibitor of FtsZ with potent and selective anti-staphylococcal activity.
|
| |
Science, 321,
1673-1675.
|
|
|
PDB code:
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E.R.Miraldi,
P.J.Thomas,
and
L.Romberg
(2008).
Allosteric models for cooperative polymerization of linear polymers.
|
| |
Biophys J, 95,
2470-2486.
|
|
|
|
|
|
|
F.van den Ent,
T.M.Vinkenvleugel,
A.Ind,
P.West,
D.Veprintsev,
N.Nanninga,
T.den Blaauwen,
and
J.Löwe
(2008).
Structural and mutational analysis of the cell division protein FtsQ.
|
| |
Mol Microbiol, 68,
110-123.
|
|
|
PDB codes:
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|
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G.Ebersbach,
E.Galli,
J.Møller-Jensen,
J.Löwe,
and
K.Gerdes
(2008).
Novel coiled-coil cell division factor ZapB stimulates Z ring assembly and cell division.
|
| |
Mol Microbiol, 68,
720-735.
|
|
|
|
|
|
|
G.Lan,
A.Dajkovic,
D.Wirtz,
and
S.X.Sun
(2008).
Polymerization and bundling kinetics of FtsZ filaments.
|
| |
Biophys J, 95,
4045-4056.
|
|
|
|
|
|
|
I.K.Cann
(2008).
Cell sorting protein homologs reveal an unusual diversity in archaeal cell division.
|
| |
Proc Natl Acad Sci U S A, 105,
18653-18654.
|
|
|
|
|
|
|
J.Pogliano
(2008).
The bacterial cytoskeleton.
|
| |
Curr Opin Cell Biol, 20,
19-27.
|
|
|
|
|
|
|
K.Kanoh,
K.Adachi,
S.Matsuda,
Y.Shizuri,
K.Yasumoto,
T.Kusumi,
K.Okumura,
and
T.Kirikae
(2008).
New sulfoalkylresorcinol from marine-derived fungus, Zygosporium sp. KNC52.
|
| |
J Antibiot (Tokyo), 61,
192-194.
|
|
|
|
|
|
|
L.M.Rice,
E.A.Montabana,
and
D.A.Agard
(2008).
The lattice as allosteric effector: structural studies of alphabeta- and gamma-tubulin clarify the role of GTP in microtubule assembly.
|
| |
Proc Natl Acad Sci U S A, 105,
5378-5383.
|
|
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PDB code:
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|
|
L.Niu,
and
J.Yu
(2008).
Investigating intracellular dynamics of FtsZ cytoskeleton with photoactivation single-molecule tracking.
|
| |
Biophys J, 95,
2009-2016.
|
|
|
|
|
|
|
M.Pilhofer,
K.Rappl,
C.Eckl,
A.P.Bauer,
W.Ludwig,
K.H.Schleifer,
and
G.Petroni
(2008).
Characterization and evolution of cell division and cell wall synthesis genes in the bacterial phyla Verrucomicrobia, Lentisphaerae, Chlamydiae, and Planctomycetes and phylogenetic comparison with rRNA genes.
|
| |
J Bacteriol, 190,
3192-3202.
|
|
|
|
|
|
|
M.Thanbichler,
and
L.Shapiro
(2008).
Getting organized--how bacterial cells move proteins and DNA.
|
| |
Nat Rev Microbiol, 6,
28-40.
|
|
|
|
|
|
|
R.Jaiswal,
and
D.Panda
(2008).
Cysteine 155 plays an important role in the assembly of Mycobacterium tuberculosis FtsZ.
|
| |
Protein Sci, 17,
846-854.
|
|
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|
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R.L.Lock,
and
E.J.Harry
(2008).
Cell-division inhibitors: new insights for future antibiotics.
|
| |
Nat Rev Drug Discov, 7,
324-338.
|
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|
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|
|
R.Srinivasan,
M.Mishra,
L.Wu,
Z.Yin,
and
M.K.Balasubramanian
(2008).
The bacterial cell division protein FtsZ assembles into cytoplasmic rings in fission yeast.
|
| |
Genes Dev, 22,
1741-1746.
|
|
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|
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|
|
T.Läppchen,
V.A.Pinas,
A.F.Hartog,
G.J.Koomen,
C.Schaffner-Barbero,
J.M.Andreu,
D.Trambaiolo,
J.Löwe,
A.Juhem,
A.V.Popov,
and
T.den Blaauwen
(2008).
Probing FtsZ and tubulin with C8-substituted GTP analogs reveals differences in their nucleotide binding sites.
|
| |
Chem Biol, 15,
189-199.
|
|
|
PDB code:
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T.O.Yeates,
C.A.Kerfeld,
S.Heinhorst,
G.C.Cannon,
and
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R.Marrington,
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Proc Natl Acad Sci U S A, 100,
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C.W.Wolgemuth,
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J Biol Chem, 278,
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Proc Natl Acad Sci U S A, 100,
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PDB codes:
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S.Rueda,
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J.M.Andreu,
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Mol Microbiol, 44,
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Mol Microbiol, 42,
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Novel molecules that interact with microtubules and have functional activity similar to Taxol.
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Structure, 8,
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PDB code:
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D.J.Scheffers,
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Acta Crystallogr D Biol Crystallogr, 56,
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PDB code:
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