Backbone dynamics of the functional domain of Paracoccus denitrificans
Cytochrome c552 in the Reduced state

SWISS-PROT P54820 'CYTOCHROME C-552'
This deposit represents the soluble fragment containing the
functional domain which starts at position 78 and is preceded
by an additional Met residue.

electron-transfer mediator in bacterial respiratory chain

This deposit represents the soluble fragment containing the
functional domain which starts at position 78 and is preceded
by an additional Met residue.

solution structure of reduced cytochrome c552

solution structure of oxidized cytochrome c552

Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Wed Jul 20 15:50:33 2011

3,3'-(7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-diyl)dipropanoic acid

3-[(5Z,10Z,14Z,19Z)-18-(2-carboxyethyl)-8,13-bis(ethenyl)-3,7,12,17-tetramethyl-21,23-dihydroporphyrin-2-yl]propanoic acid

Solution structure and dynamics of the functional domain of Paracoccus denitrificans cytochrome c(552) in both redox states.

Pristovsek, P., Luecke, C., Reincke, B., Loehr, F., Ludwig, B. & Rueterjans, H.
(2000). Complete 1H, 15N and 13C assignment of the functional domain of
Paracoccus denitrificans cytochrome c552 in the reduced state.
J. Biomol. NMR, 16, 353-354.

Complete 1H, 15N and 13C assignment of the functional domain of paracoccus denitrificans cytochrome c552 in the reduced state.

In order to determine the solution structure of Paracoccus denitrificans
cytochrome c552 by NMR, we cloned and isotopically labeled a 10.5-kDa soluble
fragment (100 residues) containing the functional domain of the 18.2-kDa
membrane-bound protein. Using uniformly 15N-enriched samples of cytochrome c552
in the reduced state, a variety of two-dimensional and three-dimensional
heteronuclear double-resonance NMR experiments was employed to achieve complete
1H and 15N assignments. A total of 1893 distance restraints was derived from
homonuclear 2D-NOESY and heteronuclear 3D-NOESY spectra; 1486 meaningful
restraints were used in the structure calculations. After restrained energy
minimization a family of 20 structures was obtained with rmsd values of 0.56
+/- 0. 10 A and 1.09 +/- 0.09 A for the backbone and heavy atoms, respectively.
The overall topology is similar to that seen in previously reported models of
this class of proteins. The global fold consists of two long helices at the
N-terminus and C-terminus and three shorter helices surrounding the heme
moiety; the helices are connected by well-defined loops. Comparison with the
X-ray structure shows some minor differences in the positions of the Trp57 and
Phe65 side-chain rings as well as the heme propionate groups.

Pristovsek, P., Luecke, C., Reincke, B., Ludwig, B. & Rueterjans, H. (2000)
Solution structure of the functional domain of Paracoccus denitrificans
cytochrome c552 in the reduced state.
Eur. J. Biochem. 267, 4205-4212.

Solution structure of the functional domain of Paracoccus denitrificans cytochrome c552 in the reduced state.

A membrane-bound c-type cytochrome, c552, acts as the electron mediator between
the cytochrome bc1 complex and cytochrome c oxidase in the branched respiratory
chain of the bacterium Paracoccus denitrificans. Unlike in mitochondria where a
soluble cytochrome c interacts with both complexes, the bacterial c552, the
product of the cycM gene, shows a tripartite structure, with an N-terminal
membrane anchor separated from a typical class I cytochrome domain by a highly
charged region. Two derivative fragments, lacking either only the membrane
spanning region or both N-terminal domains, were constructed on the genetic
level, and expressed in Escherichia coli cotransformed with the ccm gene
cluster encoding host-specific cytochrome c maturation factors. High levels of
cytochromes c were expressed and located in the periplasm as holo-proteins;
both these purified c552 fragments are functional in electron transport to
oxidase, as ascertained by kinetic measurements, and will prove useful for
future structural studies of complex formation by NMR and X-ray diffraction.

Reincke, B., Thoeny-Meyer, L., Dannehl, C., Odenwald,
A., Aidim, M., Witt, H., Rueterjans, H. & Ludwig, B. (1999) Heterologous
expression of soluble fragments of cytochrome c552 acting as electron donor to
the Paracoccus denitrificans cytochrome c oxidase.
Biochim. Biophys. Acta, 1441, 114-120.

Heterologous expression of soluble fragments of cytochrome c552 acting as electron donor to the Paracoccus denitrificans cytochrome c oxidase.

Unlike mitochondria, many bacteria use a large repertoire of c-type cytochromes
in different branches of their electron transport system. Among the many
cytochromes c present in the soil bacterium Paracoccus denitrificans, a
membrane-bound cytochrome (c552) has been suggested to mediate the electron
transport between the cytochrome bc1 complex and cytochrome-c oxidase [Berry,
E. A. & Trumpower, B. L. (1985) J. Biol. Chem. 260, 2458-2467]. We have
purified this cytochrome from cytoplasmic membranes, and cloned and sequenced
its gene, cycM. Sequence analysis reveals that, while its C-terminal portion is
highly similar to type-I cytochromes c, its N-terminal part contains a
hydrophobic segment providing membrane attachment. In addition, we present
immunological evidence for its functional role in respiration.

Turba, A., Jetzek, M. & Ludwig, B. (1995) Purification
of Paracoccus denitrificans cytochrome c552 and sequence analysis of the gene.
Eur. J. Biochem., 231, 259-265.

Purification of Paracoccus denitrificans cytochrome c552 and sequence analysis of the gene.

Paracoccus denitrificans cytochrome c552, soluble fragment

Solution Structure Of The Functional Domain Of Paracoccus Denitrificans Cytochrome C552 In The Oxidized State

Structure Of The Soluble Domain Of Cytochrome C552 From Paracoccus Denitrificans In The Reduced State

Structure Of The Soluble Domain Of Cytochrome C552 From Paracoccus Denitrificans In The Oxidised State

Structure Of The Soluble Domain Of Cytochrome C552 With Its Flexible Linker Segment From Paracoccus Denitrificans

cytochrome C552 [Paracoccus denitrificans]

cytochrome c, class I [Paracoccus denitrificans PD1222]

RecName: Full=Cytochrome c-552; AltName: Full=Cytochrome c552 [Paracoccus denitrificans]

chemical shift assignments of reduced cytochrome c552

chemical shift assignments of oxidized cytochrome c552

small excess sodium dithionite as reducing agent