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PDBsum entry 1cxy
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Electron transport
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PDB id
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1cxy
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Electron transport
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Title:
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Structure and characterization of ectothiorhodospira vacuolata cytochrome b558, a prokaryotic homologue of cytochrome b5
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Structure:
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Cytochrome b5. Chain: a. Engineered: yes
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Source:
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Ectothiorhodospira shaposhnikovii. Organism_taxid: 1054. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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1.65Å
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R-factor:
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0.186
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R-free:
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0.220
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Authors:
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V.Kostanjevecki,D.Leys,G.Van Driessche,T.E.Meyer,M.A.Cusanovich, U.Fischer,Y.Guisez,J.Van Beeumen
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Key ref:
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V.Kostanjevecki
et al.
(1999).
Structure and characterization of Ectothiorhodospira vacuolata cytochrome b(558), a prokaryotic homologue of cytochrome b(5).
J Biol Chem,
274,
35614-35620.
PubMed id:
DOI:
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Date:
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31-Aug-99
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Release date:
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10-Sep-99
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PROCHECK
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Headers
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References
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P82291
(CYB5_ECTSH) -
Soluble cytochrome b558 from Ectothiorhodospira shaposhnikovii
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Seq:
Struc:
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91 a.a.
81 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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J Biol Chem
274:35614-35620
(1999)
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PubMed id:
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Structure and characterization of Ectothiorhodospira vacuolata cytochrome b(558), a prokaryotic homologue of cytochrome b(5).
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V.Kostanjevecki,
D.Leys,
G.Van Driessche,
T.E.Meyer,
M.A.Cusanovich,
U.Fischer,
Y.Guisez,
J.Van Beeumen.
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ABSTRACT
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A soluble cytochrome b(558) from the purple phototropic bacterium
Ectothiorhodospira vacuolata was completely sequenced by a combination of
automated Edman degradation and mass spectrometry. The protein, with a measured
mass of 10,094.7 Da, contains 90 residues and binds a single protoheme.
Unexpectedly, the sequence shows homology to eukaryotic cytochromes b(5). As no
prokaryotic homologue had been reported so far, we developed a protocol for the
expression, purification, and crystallization of recombinant cytochrome b(558).
The structure was solved by molecular replacement to a resolution of 1.65 A. It
shows that cytochrome b(558) is indeed the first bacterial cytochrome b(5) to be
characterized and differs from its eukaryotic counterparts by the presence of a
disulfide bridge and a four-residue insertion in front of the sixth ligand
(histidine). Eukaryotes contain a variety of b(5) homologues, including soluble
and membrane-bound multifunctional proteins as well as multidomain enzymes such
as sulfite oxidase, fatty-acid desaturase, nitrate reductase, and lactate
dehydrogenase. A search of the Mycobacterium tuberculosis genome showed that a
previously unidentified gene encodes a fatty-acid desaturase with an N-terminal
b(5) domain. Thus, it may provide another example of a bacterial b(5) homologue.
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Selected figure(s)
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Figure 4.
Fig. 4. Detail of the weighted 2F[o]  F[c]
electron density map surrounding the heme group and both heme
ligands with the final model superposed.
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Figure 8.
Fig. 8. Comparison of the electrostatic molecular
surfaces around the heme pockets of cytochromes b[558] (A) and
b[5] (B). The surface is colored according to the electrostatic
potential (red, negative; blue, positive) and made transparent;
the heme group is blue. This figure was generated by GRASP (41).
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(1999,
274,
35614-35620)
copyright 1999.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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C.Gostincar,
M.Turk,
and
N.Gunde-Cimerman
(2010).
The evolution of fatty acid desaturases and cytochrome b5 in eukaryotes.
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J Membr Biol,
233,
63-72.
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H.Diemer,
M.Elias,
F.Renault,
D.Rochu,
C.Contreras-Martel,
C.Schaeffer,
A.Van Dorsselaer,
and
E.Chabriere
(2008).
Tandem use of X-ray crystallography and mass spectrometry to obtain ab initio the complete and exact amino acids sequence of HPBP, a human 38-kDa apolipoprotein.
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Proteins,
71,
1708-1720.
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PDB code:
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L.Min,
N.V.Strushkevich,
I.N.Harnastai,
H.Iwamoto,
A.A.Gilep,
H.Takemori,
S.A.Usanov,
Y.Nonaka,
H.Hori,
G.P.Vinson,
and
M.Okamoto
(2005).
Molecular identification of adrenal inner zone antigen as a heme-binding protein.
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FEBS J,
272,
5832-5843.
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W.Mifsud,
and
A.Bateman
(2002).
Membrane-bound progesterone receptors contain a cytochrome b5-like ligand-binding domain.
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Genome Biol,
3,
RESEARCH0068.
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C.S.Miles,
T.W.Ost,
M.A.Noble,
A.W.Munro,
and
S.K.Chapman
(2000).
Protein engineering of cytochromes P-450.
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Biochim Biophys Acta,
1543,
383-407.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
