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PDBsum entry 2uxt
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Oxidoreductase
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PDB id
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2uxt
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References listed in PDB file
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Key reference
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Title
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The escherichia coli cell division protein and model tat substrate sufi (ftsp) localizes to the septal ring and has a multicopper oxidase-Like structure.
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Authors
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M.Tarry,
S.J.Arends,
P.Roversi,
E.Piette,
F.Sargent,
B.C.Berks,
D.S.Weiss,
S.M.Lea.
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Ref.
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J Mol Biol, 2009,
386,
504-519.
[DOI no: ]
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PubMed id
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Abstract
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The Escherichia coli protein SufI (FtsP) has recently been proposed to be a
component of the cell division apparatus. The SufI protein is also in widespread
experimental use as a model substrate in studies of the Tat (twin arginine
translocation) protein transport system. We have used SufI-GFP (green
fluorescent protein) fusions to show that SufI localizes to the septal ring in
the dividing cell. We have also determined the structure of SufI by X-ray
crystallography to a resolution of 1.9 A. SufI is structurally related to the
multicopper oxidase superfamily but lacks metal cofactors. The structure of SufI
suggests it serves a scaffolding rather than an enzymatic role in the septal
ring and reveals regions of the protein likely to be involved in the
protein-protein interactions required to assemble SufI at the septal ring.
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Figure 4.
Fig. 4. Structure of SufI. (a) Cartoon representation of
SufI. The structure shown is for chain A of the orthorhombic
space group with domain 1 shown in red, domain 2 in green and
domain 3 in blue. Regions of missing density are shown as black
dotted lines. The arrow in the region of missing density
indicates where the protein is subject to proteolytic cleavage.
(b) Stereo view showing CueO (blue) overlaid on the orthorhombic
SufI (red) structure. PDB ID 1KV7 was overlaid onto the
orthorhombic chain A of SufI with the program CCP4-Lsqkab. The
positions of the N- and C-termini of the proteins are shown and
the tower region of CueO is labelled for reference. The
orientation is as in (a). (c) Stereo view showing representative
electron density (2F[o] − F[c]) of orthorhombic chain A,
residues 107–131 contoured at 1σ. The positions of the
invariant residues leucine 112, arginine 118, tryptophan 126 and
proline 128 are labelled.
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Figure 7.
Fig. 7. Identification and localization of conserved residues
in SufI. (a) CueO: the conserved residues Gly113 and Gly114
(green sticks) sit above the trinuclear copper centre (shown as
transparent spheres). Residues Gly117, Arg125 and Val127 (blue
sticks) form the brim of a surface cavity that exposes the
112–114 loop (DGG in CueO, conserved as DGX across all
multicopper oxidases) to the solvent. (b) SufI: in green, the
glycine residues Gly114 and Gly115 corresponding to the glycines
in (a); in blue, the residues Arg118, Trp126 and Pro128, which
are all highly conserved across SufI sequences and prevent
solvent access to the 112–114 loop in the SufI structure. (c)
A surface representation of SufI, coloured red (surface residue
most conserved) through orange, yellow, and green, to blue
(least conserved). The N- and C-termini of the protein are shown
for reference and highly conserved surface residues are
labelled. A black star marks the location of the residues
118–128 that cover the pocket corresponding to the CueO
catalytic centre. The right-hand panel shows a second view of
the SufI surface, rotated with respect to the left-hand panel by
180° around the vertical axis.
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The above figures are
reprinted
from an Open Access publication published by Elsevier:
J Mol Biol
(2009,
386,
504-519)
copyright 2009.
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