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PDBsum entry 3mcd
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* Residue conservation analysis
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PDB id:
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Cell cycle
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Title:
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Crystal structure of helicobacter pylori mine, a cell division topological specificity factor
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Structure:
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Cell division topological specificity factor. Chain: a, b. Engineered: yes
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Source:
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Helicobacter pylori. Campylobacter pylori. Organism_taxid: 210. Gene: mine, hp_0332. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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3.20Å
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R-factor:
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0.271
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R-free:
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0.303
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Authors:
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G.B.Kang,H.E.Song,M.K.Kim,H.S.Youn,J.G.Lee,J.Y.An,H.Jeon,J.S.Chun, S.H.Eom
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Key ref:
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G.B.Kang
et al.
(2010).
Crystal structure of Helicobacter pylori MinE, a cell division topological specificity factor.
Mol Microbiol,
76,
1222-1231.
PubMed id:
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Date:
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29-Mar-10
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Release date:
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05-May-10
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PROCHECK
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Headers
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References
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Enzyme class:
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Chains A, B:
E.C.?
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Mol Microbiol
76:1222-1231
(2010)
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PubMed id:
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Crystal structure of Helicobacter pylori MinE, a cell division topological specificity factor.
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G.B.Kang,
H.E.Song,
M.K.Kim,
H.S.Youn,
J.G.Lee,
J.Y.An,
J.S.Chun,
H.Jeon,
S.H.Eom.
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ABSTRACT
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In Gram-negative bacteria, proper placement of the FtsZ ring, mediated by
nucleoid occlusion and the activities of the dynamic oscillating Min proteins
MinC, MinD and MinE, is required for correct positioning of the cell division
septum. MinE is a topological specificity factor that counters the activity of
MinCD division inhibitor at the mid-cell division site. Its structure consists
of an anti-MinCD domain and a topology specificity domain (TSD). Previous NMR
analysis of truncated Escherichia coli MinE showed that the TSD domain contains
a long alpha-helix and two anti-parallel beta-strands, which mediate formation
of a homodimeric alpha/beta structure. Here we report the crystal structure of
full-length Helicobacter pylori MinE and redefine its TSD based on that
structure. The N-terminal region of the TSD (residues 19-26), previously defined
as part of the anti-MinCD domain, forms a beta-strand (betaA) and participates
in TSD folding. In addition, H. pylori MinE forms a dimer through the
interaction of anti-parallel betaA-strands. Moreover, we observed serial
dimer-dimer interactions within the crystal packing, resulting in the formation
of a multimeric structure. We therefore redefine the functional domain of MinE
and propose that a multimeric filamentous structure is formed through
anti-parallel beta-strand interactions.
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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.Loose,
K.Kruse,
and
P.Schwille
(2011).
Protein self-organization: lessons from the min system.
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Annu Rev Biophys,
40,
315-336.
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W.Wu,
K.T.Park,
T.Holyoak,
and
J.Lutkenhaus
(2011).
Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC.
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Mol Microbiol,
79,
1515-1528.
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PDB code:
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H.Ghasriani,
T.Ducat,
C.T.Hart,
F.Hafizi,
N.Chang,
A.Al-Baldawi,
S.H.Ayed,
P.Lundström,
J.A.Dillon,
and
N.K.Goto
(2010).
Appropriation of the MinD protein-interaction motif by the dimeric interface of the bacterial cell division regulator MinE.
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Proc Natl Acad Sci U S A,
107,
18416-18421.
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PDB code:
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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
