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PDBsum entry 4l1c
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Protein binding
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PDB id
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4l1c
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References listed in PDB file
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Key reference
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Title
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Crystal structure of the n-Terminal domain of minc dimerized via domain swapping.
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Authors
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J.Y.An,
T.G.Kim,
K.R.Park,
J.G.Lee,
H.S.Youn,
Y.Lee,
J.Y.Kang,
G.B.Kang,
S.H.Eom.
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Ref.
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J Synchrotron Radiat, 2013,
20,
984-988.
[DOI no: ]
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PubMed id
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Abstract
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Proper cell division at the mid-site of gram-negative bacteria reflects critical
regulation by the min system (MinC, MinD and MinE) of the cytokinetic Z ring,
which is a polymer composed of FtsZ subunits. MinC and MinD act together to
inhibit aberrantly positioned Z-ring formation. MinC consists of two domains: an
N-terminal domain (MinCNTD), which interacts with FtsZ and inhibits FtsZ
polymerization, and a C-terminal domain (MinCCTD), which interacts with MinD and
inhibits the bundling of FtsZ filaments. These two domains reportedly function
together, and both are essential for normal cell division. The full-length
dimeric structure of MinC from Thermotoga maritima has been reported, and shows
that MinC dimerization occurs via MinCCTD; MinCNTD is not involved in
dimerization. Here the crystal structure of Escherichia coli MinCNTD
(EcoMinCNTD) is reported. EcoMinCNTD forms a dimer via domain swapping between
the first β strands in each subunit. It is therefore suggested that the
dimerization of full-length EcoMinC occurs via both MinCCTD and MinCNTD, and
that the dimerized EcoMinCNTD likely plays an important role in inhibiting
aberrant Z-ring localization.
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