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PDBsum entry 1vz0
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Nuclear protein
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PDB id
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1vz0
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Contents |
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* Residue conservation analysis
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PDB id:
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Nuclear protein
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Title:
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Chromosome segregation protein spo0j from thermus thermophilus
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Structure:
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Chromosome-partitioning protein spo0j. Chain: a, b, c, d, e, f, g, h. Fragment: DNA-binding domain, residues 1-222. Engineered: yes
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Source:
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Thermus thermophilus hb27. Organism_taxid: 262724. Atcc: baa-163d. Gene: spo0c, parb, tt_c1604. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: c41
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Biol. unit:
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Dimer (from PDB file)
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Resolution:
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2.30Å
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R-factor:
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0.235
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R-free:
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0.278
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Authors:
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T.A.Leonard,P.J.G.Butler,J.Lowe
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Key ref:
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T.A.Leonard
et al.
(2004).
Structural analysis of the chromosome segregation protein Spo0J from Thermus thermophilus.
Mol Microbiol,
53,
419-432.
PubMed id:
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Date:
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12-May-04
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Release date:
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19-Jul-04
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PROCHECK
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Headers
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References
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Q72H91
(SP0J_THET2) -
Chromosome-partitioning protein Spo0J from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)
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Seq: Struc:
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269 a.a.
187 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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Mol Microbiol
53:419-432
(2004)
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PubMed id:
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Structural analysis of the chromosome segregation protein Spo0J from Thermus thermophilus.
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T.A.Leonard,
P.J.Butler,
J.Löwe.
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ABSTRACT
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Prokaryotic chromosomes and plasmids encode partitioning systems that are
required for DNA segregation at cell division. The plasmid partitioning loci
encode two proteins, ParA and ParB, and a cis-acting centromere-like site
denoted parS. The chromosomally encoded homologues of ParA and ParB, Soj and
Spo0J, play an active role in chromosome segregation during bacterial cell
division and sporulation. Spo0J is a DNA-binding protein that binds to parS
sites in vivo. We have solved the X-ray crystal structure of a C-terminally
truncated Spo0J (amino acids 1-222) from Thermus thermophilus to 2.3 A
resolution by multiwavelength anomalous dispersion. It is a DNA-binding protein
with structural similarity to the helix-turn-helix (HTH) motif of the lambda
repressor DNA-binding domain. The crystal structure is an antiparallel dimer
with the recognition alpha-helices of the HTH motifs of each monomer separated
by a distance of 34 A corresponding to the length of the helical repeat of
B-DNA. Sedimentation velocity and equilibrium ultracentrifugation studies show
that full-length Spo0J exists in a monomer-dimer equilibrium in solution and
that Spo0J1-222 is exclusively monomeric. Sedimentation of the C-terminal domain
of Spo0J shows it to be exclusively dimeric, confirming that the C-terminus is
the primary dimerization domain. We hypothesize that the C-terminus mediates
dimerization of Spo0J, thereby effectively increasing the local concentration of
the N-termini, which most probably dimerize, as shown by our structure, upon
binding to a cognate parS site.
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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.N.Chaudhuri,
S.Gupta,
V.S.Urban,
M.R.Chance,
R.D'Mello,
L.Smith,
K.Lyons,
and
J.Gee
(2011).
A combined global and local approach to elucidate spatial organization of the Mycobacterial ParB-parS partition assembly.
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Biochemistry,
50,
1799-1807.
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L.Huang,
P.Yin,
X.Zhu,
Y.Zhang,
and
K.Ye
(2011).
Crystal structure and centromere binding of the plasmid segregation protein ParB from pCXC100.
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Nucleic Acids Res,
39,
2954-2968.
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PDB code:
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B.Ditkowski,
P.Troć,
K.Ginda,
M.Donczew,
K.F.Chater,
J.Zakrzewska-Czerwińska,
and
D.Jakimowicz
(2010).
The actinobacterial signature protein ParJ (SCO1662) regulates ParA polymerization and affects chromosome segregation and cell division during Streptomyces sporulation.
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Mol Microbiol,
78,
1403-1415.
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F.Gorrec
(2009).
The MORPHEUS protein crystallization screen.
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J Appl Crystallogr,
42,
1035-1042.
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S.Ringgaard,
J.van Zon,
M.Howard,
and
K.Gerdes
(2009).
Movement and equipositioning of plasmids by ParA filament disassembly.
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Proc Natl Acad Sci U S A,
106,
19369-19374.
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H.Murray,
and
J.Errington
(2008).
Dynamic control of the DNA replication initiation protein DnaA by Soj/ParA.
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Cell,
135,
74-84.
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N.Shaw,
W.Tempel,
J.Chang,
H.Yang,
C.Cheng,
J.Ng,
J.Rose,
Z.Rao,
B.C.Wang,
and
Z.J.Liu
(2008).
Crystal structure solution of a ParB-like nuclease at atomic resolution.
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Proteins,
70,
263-267.
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PDB code:
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A.M.Breier,
and
A.D.Grossman
(2007).
Whole-genome analysis of the chromosome partitioning and sporulation protein Spo0J (ParB) reveals spreading and origin-distal sites on the Bacillus subtilis chromosome.
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Mol Microbiol,
64,
703-718.
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F.Hayes,
and
D.Barillà
(2006).
The bacterial segrosome: a dynamic nucleoprotein machine for DNA trafficking and segregation.
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Nat Rev Microbiol,
4,
133-143.
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F.Hayes,
and
D.Barillà
(2006).
Assembling the bacterial segrosome.
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Trends Biochem Sci,
31,
247-250.
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H.Murray,
H.Ferreira,
and
J.Errington
(2006).
The bacterial chromosome segregation protein Spo0J spreads along DNA from parS nucleation sites.
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Mol Microbiol,
61,
1352-1361.
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K.A.Michie,
and
J.Löwe
(2006).
Dynamic filaments of the bacterial cytoskeleton.
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Annu Rev Biochem,
75,
467-492.
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D.Jakimowicz,
B.Gust,
J.Zakrzewska-Czerwinska,
and
K.F.Chater
(2005).
Developmental-stage-specific assembly of ParB complexes in Streptomyces coelicolor hyphae.
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J Bacteriol,
187,
3572-3580.
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G.Ebersbach,
and
K.Gerdes
(2005).
Plasmid segregation mechanisms.
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Annu Rev Genet,
39,
453-479.
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K.Doubrovinski,
and
M.Howard
(2005).
Stochastic model for Soj relocation dynamics in Bacillus subtilis.
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Proc Natl Acad Sci U S A,
102,
9808-9813.
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M.A.Schumacher,
and
B.E.Funnell
(2005).
Structures of ParB bound to DNA reveal mechanism of partition complex formation.
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Nature,
438,
516-519.
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PDB code:
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T.A.Leonard,
P.J.Butler,
and
J.Löwe
(2005).
Bacterial chromosome segregation: structure and DNA binding of the Soj dimer--a conserved biological switch.
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EMBO J,
24,
270-282.
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PDB codes:
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Y.R.Sevastsyanovich,
M.A.Titok,
R.Krasowiak,
L.E.Bingle,
and
C.M.Thomas
(2005).
Ability of IncP-9 plasmid pM3 to replicate in Escherichia coli is dependent on both rep and par functions.
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Mol Microbiol,
57,
819-833.
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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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}
}
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