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PDBsum entry 1hf2
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Cell division protein
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PDB id
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1hf2
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Contents |
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* Residue conservation analysis
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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 bacterial cell division inhibitor minc.
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Authors
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S.C.Cordell,
R.E.Anderson,
J.Löwe.
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Ref.
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EMBO J, 2001,
20,
2454-2461.
[DOI no: ]
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PubMed id
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Abstract
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Bacterial cell division requires accurate selection of the middle of the cell,
where the bacterial tubulin homologue FtsZ polymerizes into a ring structure. In
Escherichia coli, site selection is dependent on MinC, MinD and MINE: MinC acts,
with MinD, to inhibit division at sites other than the midcell by directly
interacting with FTSZ: Here we report the crystal structure to 2.2 A of MinC
from Thermotoga maritima. MinC consists of two domains separated by a short
linker. The C-terminal domain is a right-handed beta-helix and is involved in
dimer formation. The crystals contain two different MinC dimers, demonstrating
flexibility in the linker region. The two-domain architecture and dimerization
of MinC can be rationalized with a model of cell division inhibition. MinC does
not act like SulA, which affects the GTPase activity of FtsZ, and the model can
explain how MinC would select for the FtsZ polymer rather than the monomer.
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Figure 2.
Figure 2 Ribbon drawings of MinC. (A) An asymmetric unit
contains two different MinC dimers, highlighting the flexibility
of the linker region (linker, grey; N-terminal domain, yellow;
C-terminal domain, blue). Face 'A' of the triangular C-terminal
domain forms the dimer interface alone in dimer AB (top). (B)
Stereo drawing of the N-terminal domain (residues 1 -95) with
the flexible linker (residues 96 -102). (C) Top and side view of
the C-terminal domain. The domain folds into a small triangular,
right-handed  -helix
with a hydrophobic core. The length of the sides is: A, four; B,
three; and C, five residues in -conformation.
The strands in the domain have been numbered to reflect their
position with respect to the turn number and the side of the
-helix.
Made with MOLSCRIPT and RASTER3D (Kraulis, 1991; Merritt and
Bacon, 1997).
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Figure 5.
Figure 5 Structural alignment of the N-terminal domain of MinC
from T.maritima, SpoIIAA from B.subtilis (PDB 1AUZ; Kovacs et
al., 1998) and FtsA from T.maritima (PDB 1E4F; van den Ent and
Löwe, 2000). FtsA shows the highest DALI score of 3.7, r.m.s.d.
3.2 Å over 74 residues. SpoIIAA has a DALI score against the
N-terminal domain of MinC of 3.5, r.m.s.d. 3.6 Å over 72 almost
consecutive residues. Aligned stretches are coloured, all other
residues are shown in grey. Made with MOLSCRIPT and RASTER3D
(Kraulis, 1991; Merritt and Bacon, 1997).
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2001,
20,
2454-2461)
copyright 2001.
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