 |
PDBsum entry 1k3h
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Electron transport
|
PDB id
|
|
|
|
1k3h
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Nmr solution structure, Backbone mobility, And homology modeling of c-Type cytochromes from gram-Positive bacteria.
|
 |
|
Authors
|
 |
L.Banci,
I.Bertini,
S.Ciurli,
A.Dikiy,
J.Dittmer,
A.Rosato,
G.Sciara,
A.R.Thompsett.
|
 |
|
Ref.
|
 |
Chembiochem, 2002,
3,
299-310.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
 |
|
Abstract
|
 |
|
The solution structure of oxidized cytochrome c(553) (71 amino acid residues)
from the Gram-positive bacterium Bacillus pasteurii is here reported and
compared with the available crystal structure. The solution structure is
obtained from 1609 meaningful NOE data (22.7 per residue), 76 dihedral angles,
and 59 pseudocontact shifts. The root mean square deviations from the average
structure are 0.25+/-0.07 and 0.59+/-0.13 A for the backbone and all heavy
atoms, respectively, and the quality assessment of the structure is
satisfactory. The solution structure closely reproduces the fold observed in the
crystal structure. The backbone mobility was then investigated through amide
(15)N relaxation rate and (15)N-(1)H NOE measurements. The protein is rigid in
both the sub-nanosecond and millisecond time scales, probably due to the
relatively large heme:number of amino acids ratio. Modeling of eight c-type
cytochromes from other Gram-positive bacteria with a high sequence identity
(>30 %) to the present cytochrome c(553) was performed. Analysis of consensus
features accounts for the relatively low reduction potential as being due to
extensive heme hydration and indicates residues 34-35, 44-46, 69-72, and 75 as a
conserved hydrophobic patch for the interaction with a protein partner. At
variance with mitochondrial c-type cytochrome, this protein does not experience
pH-dependent coordination equilibria. The reasons for this difference are
analyzed.
|
 |
|
Secondary reference #1
|
 |
|
Title
|
 |
Crystal structure of oxidized bacillus pasteurii cytochrome c553 at 0.97-A resolution.
|
 |
|
Authors
|
 |
S.Benini,
A.González,
W.R.Rypniewski,
K.S.Wilson,
J.J.Van beeumen,
S.Ciurli.
|
 |
|
Ref.
|
 |
Biochemistry, 2000,
39,
13115-13126.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
 |
|
|
 |
|
Secondary reference #2
|
 |
|
Title
|
 |
Modulation of bacillus pasteurii cytochrome c553 reduction potential by structural and solution parameters
|
 |
|
Authors
|
 |
S.Benini,
M.Borsari,
S.Ciurli,
A.Dikiy,
M.Lamborghini.
|
 |
|
Ref.
|
 |
j biol inorg chem, 1998,
3,
371.
|
 |
 |
|
|
|
|
 |