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PDBsum entry 1k3h
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Electron transport
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PDB id
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1k3h
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Contents |
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* Residue conservation analysis
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PDB id:
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Electron transport
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Title:
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Nmr solution structure of oxidized cytochromE C-553 from bacillus pasteurii
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Structure:
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CytochromE C-553. Chain: a. Fragment: residues 22-92. Synonym: c553. Engineered: yes
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Source:
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Sporosarcina pasteurii. Organism_taxid: 1474. Expressed in: escherichia coli. Expression_system_taxid: 562.
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NMR struc:
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1 models
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Authors:
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L.Banci,I.Bertini,S.Ciurli,A.Dikiy,J.Dittmer,A.Rosato,G.Sciara, A.R.Thompsett
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Key ref:
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L.Banci
et al.
(2002).
NMR solution structure, backbone mobility, and homology modeling of c-type cytochromes from gram-positive bacteria.
Chembiochem,
3,
299-310.
PubMed id:
DOI:
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Date:
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03-Oct-01
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Release date:
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31-Oct-01
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PROCHECK
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Headers
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References
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P82599
(CY553_SPOPA) -
Cytochrome c-553 from Sporosarcina pasteurii
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Seq:
Struc:
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92 a.a.
71 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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Chembiochem
3:299-310
(2002)
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PubMed id:
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NMR solution structure, backbone mobility, and homology modeling of c-type cytochromes from gram-positive bacteria.
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L.Banci,
I.Bertini,
S.Ciurli,
A.Dikiy,
J.Dittmer,
A.Rosato,
G.Sciara,
A.R.Thompsett.
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ABSTRACT
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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.
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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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I.Bertini,
G.Cavallaro,
and
A.Rosato
(2011).
Principles and patterns in the interaction between mono-heme cytochrome c and its partners in electron transfer processes.
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Metallomics,
3,
354-362.
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M.K.Khan,
H.Rahaman,
and
F.Ahmad
(2011).
Conformation and thermodynamic stability of pre-molten and molten globule states of mammalian cytochromes-c.
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Metallomics,
3,
327-338.
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G.Kieseritzky,
G.Morra,
and
E.W.Knapp
(2006).
Stability and fluctuations of amide hydrogen bonds in a bacterial cytochrome c: a molecular dynamics study.
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J Biol Inorg Chem,
11,
26-40.
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F.Musiani,
A.Dikiy,
A.Y.Semenov,
and
S.Ciurli
(2005).
Structure of the intermolecular complex between plastocyanin and cytochrome f from spinach.
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J Biol Chem,
280,
18833-18841.
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PDB code:
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I.Bertini,
G.Cavallaro,
and
A.Rosato
(2005).
A structural model for the adduct between cytochrome c and cytochrome c oxidase.
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J Biol Inorg Chem,
10,
613-624.
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PDB code:
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J.A.Worrall,
R.E.Diederix,
M.Prudêncio,
C.E.Lowe,
S.Ciofi-Baffoni,
M.Ubbink,
and
G.W.Canters
(2005).
The effects of ligand exchange and mobility on the peroxidase activity of a bacterial cytochrome c upon unfolding.
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Chembiochem,
6,
747-758.
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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
