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PDBsum entry 1cty
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Electron transport (heme protein)
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PDB id
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1cty
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References listed in PDB file
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Key reference
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Title
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Mutation of tyrosine-67 to phenylalanine in cytochrome c significantly alters the local heme environment.
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Authors
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A.M.Berghuis,
J.G.Guillemette,
M.Smith,
G.D.Brayer.
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Ref.
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J Mol Biol, 1994,
235,
1326-1341.
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
84%.
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Abstract
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The high resolution three-dimensional atomic structures of the reduced and
oxidized states of the Y67F variant of yeast iso-1-cytochrome c have been
completed. The conformational differences observed are localized directly in the
mutation site and in the region about the pyrrole A propionate. Shifts in atomic
positions are largely restricted to nearby amino acid side-chains, whereas
little perturbation of the polypeptide chain backbone is observed. One prominent
difference between the variant and wild-type structures involves a substantial
increase in the size of an already existing internal cavity adjacent to residue
67. This same cavity contains an internally bound water molecule (Wat166), which
is found in all eukaryotic cytochromes c for which structures are available. In
the reduced Y67F mutant protein a second water molecule (Wat300) is observed to
reside in this enlarged internal cavity, assuming a position approximately
equivalent to that of the hydroxyl group of Tyr67 in the wild-type protein. A
further consequence of this mutation is the alteration of the hydrogen bond
network between Tyr67, Wat166 and other nearby residues. This appears to be
responsible for the absence of oxidation state dependent changes in polypeptide
chain flexibility observed in the wild-type protein. Furthermore, loss of the
normally resident Tyr67 OH to Met80 SD hydrogen bond leads to a significantly
lower midpoint reduction potential. These results reaffirm proposals that both
Tyr67 and Wat166 play a central role in stabilizing the alternative oxidation
states of cytochrome c.
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Secondary reference #1
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Title
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Oxidation state-Dependent conformational changes in cytochrome c.
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Authors
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A.M.Berghuis,
G.D.Brayer.
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Ref.
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J Mol Biol, 1992,
223,
959-976.
[DOI no: ]
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PubMed id
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Figure 3.
Figure 3. A schemtic representation of the atomic
skeleton of the heme group f cytochrome c and the atom
labeling convention used herein.
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Figure 10.
Figure 10. Drawings of the egion about the pyrrole
ing A propionate group in (a) reduced and (b) oxidized
yeast iso-l-cytochrome c, illustrating the positional shifts
nd altered hydrogen bonding patterns observed. The
yrrole ring A propionate group is hihlighted with dark
haded balls. Hydrogen bonds are indicated by hin
otted lines. The 2 internally bound water molecules,
Watl21 and -168, which mediate the interaction of Arg38
ith this heme propionate, are shown with largr spheres.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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Secondary reference #2
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Title
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High-Resolution refinement of yeast iso-1-Cytochrome c and comparisons with other eukaryotic cytochromes c.
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Authors
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G.V.Louie,
G.D.Brayer.
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Ref.
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J Mol Biol, 1990,
214,
527-555.
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PubMed id
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Secondary reference #3
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Title
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A polypeptide chain-Refolding event occurs in the gly82 variant of yeast iso-1-Cytochrome c.
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Authors
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G.V.Louie,
G.D.Brayer.
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Ref.
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J Mol Biol, 1989,
210,
313-322.
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PubMed id
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Secondary reference #4
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Title
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Crystallization of yeast iso-2-Cytochrome c using a novel hair seeding technique.
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Authors
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C.J.Leung,
B.T.Nall,
G.D.Brayer.
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Ref.
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J Mol Biol, 1989,
206,
783-785.
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PubMed id
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Secondary reference #5
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Title
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Yeast iso-1-Cytochrome c. A 2.8 a resolution three-Dimensional structure determination.
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Authors
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G.V.Louie,
W.L.Hutcheon,
G.D.Brayer.
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Ref.
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J Mol Biol, 1988,
199,
295-314.
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PubMed id
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Secondary reference #6
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Title
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Role of phenylalanine-82 in yeast iso-1-Cytochrome c and remote conformational changes induced by a serine residue at this position.
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Authors
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G.V.Louie,
G.J.Pielak,
M.Smith,
G.D.Brayer.
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Ref.
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Biochemistry, 1988,
27,
7870-7876.
[DOI no: ]
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PubMed id
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