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PDBsum entry 1bbh
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Electron transport(heme protein)
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PDB id
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1bbh
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Contents |
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* Residue conservation analysis
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J Mol Biol
234:433-445
(1993)
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PubMed id:
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Atomic structure of a cytochrome c' with an unusual ligand-controlled dimer dissociation at 1.8 A resolution.
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Z.Ren,
T.Meyer,
D.E.McRee.
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ABSTRACT
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The crystallographic structure of cytochrome c' from the purple phototrophic
bacterium Chromatium vinosum (CVCP) has been determined at 1.8 A resolution
using multiple isomorphous replacement. The molecule is a dimer, with each
131-residue chain folding as a four-helical bundle incorporating a covalently
bound heme group at the core. This structure is the third of the ubiquitous
cytochromes c' to be solved and is similar to the known structures of cytochrome
c' from R. molischianum (RMCP) and R. rubrum (RRCP). CVCP is unique in
exhibiting ligand-controlled dimer dissociation while RMCP and RRCP do not. The
Tyr16 side-chain, which replaced Met16 in RMCP and Leu14 in RRCP, is parallel to
the heme plane and located directly above the sixth ligand site of the heme Fe.
Any ligand binding to this site, such as CO or CN-, must move the Tyr16
side-chain, which would be expected to cause other conformational changes of
helix A, which contributes to the dimer interface, and consequently disrupting
the dimer. Thus, the crystallographic structure of CVCP suggests a mechanism for
dimer dissociation upon ligand binding. The dimer interface specificity is due
to a lock and key shape complementarity of hydrophobic residues and not to any
charge complementarity or cross-interface hydrogen bonds as is common in other
protein-protein interfaces. The co-ordinates have been deposited in the
Brookhaven Data Bank (entry P1BBH).
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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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E.Krissinel
(2011).
Macromolecular complexes in crystals and solutions.
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Acta Crystallogr D Biol Crystallogr,
67,
376-385.
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E.Krissinel
(2010).
Crystal contacts as nature's docking solutions.
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J Comput Chem,
31,
133-143.
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S.N.Wanasundara,
and
M.Thachuk
(2007).
Theoretical investigations of the dissociation of charged protein complexes in the gas phase.
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J Am Soc Mass Spectrom,
18,
2242-2253.
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T.H.Evers,
J.L.van Dongen,
E.W.Meijer,
and
M.Merkx
(2007).
Ligand-induced monomerization of Allochromatium vinosum cytochrome c' studied using native mass spectrometry and fluorescence resonance energy transfer.
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J Biol Inorg Chem,
12,
919-928.
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Y.Y.Londer,
I.S.Dementieva,
C.A.D'Ausilio,
P.R.Pokkuluri,
and
M.Schiffer
(2006).
Characterization of a c-type heme-containing PAS sensor domain from Geobacter sulfurreducens representing a novel family of periplasmic sensors in Geobacteraceae and other bacteria.
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FEMS Microbiol Lett,
258,
173-181.
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C.Cole,
and
J.Warwicker
(2002).
Side-chain conformational entropy at protein-protein interfaces.
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Protein Sci,
11,
2860-2870.
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D.M.Lawson,
C.E.Stevenson,
C.R.Andrew,
and
R.R.Eady
(2000).
Unprecedented proximal binding of nitric oxide to heme: implications for guanylate cyclase.
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EMBO J,
19,
5661-5671.
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PDB codes:
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R.Cross,
J.Aish,
S.J.Paston,
R.K.Poole,
and
J.W.Moir
(2000).
Cytochrome c' from Rhodobacter capsulatus confers increased resistance to nitric oxide.
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J Bacteriol,
182,
1442-1447.
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B.D.Howes,
C.B.Schiodt,
K.G.Welinder,
M.P.Marzocchi,
J.G.Ma,
J.Zhang,
J.A.Shelnutt,
and
G.Smulevich
(1999).
The quantum mixed-spin heme state of barley peroxidase: A paradigm for class III peroxidases.
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Biophys J,
77,
478-492.
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J.W.Moir
(1999).
Cytochrome c' from Paracoccus denitrificans: spectroscopic studies consistent with a role for the protein in nitric oxide metabolism.
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Biochim Biophys Acta,
1430,
65-72.
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S.Benini,
W.R.Rypniewski,
K.S.Wilson,
and
S.Ciurli
(1998).
Crystallization and preliminary X-ray diffraction analysis of cytochrome c' from Rubrivivax gelatinosus at 1.3 A resolution.
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Acta Crystallogr D Biol Crystallogr,
54,
284-287.
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J.A.Zahn,
D.M.Arciero,
A.B.Hooper,
and
A.A.Dispirito
(1996).
Cytochrome c' of Methylococcus capsulatus Bath.
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Eur J Biochem,
240,
684-691.
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T.H.Tahirov,
S.Misaki,
T.E.Meyer,
M.A.Cusanovich,
Y.Higuchi,
and
N.Yasuoka
(1996).
Concerted movement of side chains in the haem vicinity observed on ligand binding in cytochrome c' from rhodobacter capsulatus.
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Nat Struct Biol,
3,
459-464.
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PDB code:
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A.Shaw,
P.A.Fortes,
C.D.Stout,
and
V.D.Vacquier
(1995).
Crystal structure and subunit dynamics of the abalone sperm lysin dimer: egg envelopes dissociate dimers, the monomer is the active species.
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J Cell Biol,
130,
1117-1125.
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PDB code:
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M.T.Even,
R.J.Kassner,
M.Dolata,
T.E.Meyer,
and
M.A.Cusanovich
(1995).
Molecular cloning and sequencing of cytochrome c' from the phototrophic purple sulfur bacterium Chromatium vinosum.
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Biochim Biophys Acta,
1231,
220-222.
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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
codes are
shown on the right.
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