 |
PDBsum entry 3dp5
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Electron transport
|
PDB id
|
|
|
|
3dp5
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Crystal packing of the c(6)-Type cytochrome omcf from geobacter sulfurreducens is mediated by an n-Terminal strep-Tag ii.
|
|
|
Authors
|
|
P.Lukat,
M.Hoffmann,
O.Einsle.
|
|
|
Ref.
|
|
Acta Crystallogr D Biol Crystallogr, 2008,
64,
919-926.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The putative outer membrane c-type cytochrome OmcF from Geobacter sulfurreducens
contains a single haem group and shows homology to soluble cytochromes c(6), a
class of electron-transfer proteins that are typically found in cyanobacterial
photosynthetic electron-transfer chains. OmcF was overexpressed heterologously
in Escherichia coli as an N-terminal Strep-tag II fusion protein and isolated
using streptactin-affinity chromatography followed by size-exclusion
chromatography. The structure was solved by Fe SAD using data collected to a
resolution of 1.86 A on a rotating copper-anode X-ray generator. In the crystal,
packing interactions in one dimension were exclusively mediated through the
Strep-tag II sequence. The tag and linker regions were in contact with three
further monomers of OmcF, leading to a well defined electron-density map for
this engineered and secondary-structure-free region of the molecule.
|
|
|
|
|
|
|
|
Figure 4.
Figure 4 Stereo representation of the cytochrome c[6] domain of
G. sulfurreducens OmcF. The single haem group of OmcF is
covalently linked to the peptide chain via a bonding motif with
sequence CAGCH (residues 35-39). His39 functions as a proximal
axial ligand to the haem Fe atom, while the distal axial ligand
is Met79. Every tenth residue in the sequence is marked.
|
|
Figure 7.
Figure 7 Stereo representation showing the interactions of the
linker (blue) and Strep-tag II region (red) with three
neighbouring monomers as detailed in Table 3-. Hydrogen-bonding
interactions within the linker/tag are shown in blue and
interactions with other monomers in red. Five of the seven
observed hydrogen-bonding interactions are formed by the
Strep-tag II and the other two are formed by the linker region.
|
|
|
|
|
|
The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2008,
64,
919-926)
copyright 2008.
|
|
|
|
|
|
|
