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PDBsum entry 1fcs
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Oxygen transport
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PDB id
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1fcs
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References listed in PDB file
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Key reference
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Title
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Crystal structure of a distal site double mutant of sperm whale myoglobin at 1.6 a resolution.
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Authors
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M.Rizzi,
M.Bolognesi,
A.Coda,
F.Cutruzzolà,
C.T.Allocatelli,
A.Brancaccio,
M.Brunori.
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Ref.
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FEBS Lett, 1993,
320,
13-16.
[DOI no: ]
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PubMed id
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Abstract
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The three-dimensional structure of sperm whale myoglobin
His64(E7)-->Val,Thr67(E10)-->Arg double mutant has been studied by X-ray
crystallography at 1.6 A resolution, and refined to a crystallographic R-factor
of 0.197. The Arg67(E10) side chain is extended in the direction of the ligand
binding site, and its NH1 atom is at a distance of 3.11 A from the NH1 atom of
Arg45(CD3), which is also pointing towards the distal site. Both are kept in
this position by hydrogen bonding and electrostatic interactions with a solvent
sulfate ion, located amongst the two, on the protein surface. No liganded water
molecule is present at the sixth coordination position of the Fe(III) heme.
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Secondary reference #1
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Title
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Control and recognition of anionic ligands in myoglobin.
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Authors
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F.Cutruzzolà,
C.T.Allocatelli,
P.Ascenzi,
M.Bolognesi,
S.G.Sligar,
M.Brunori.
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Ref.
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Febs Lett, 1991,
282,
281-284.
[DOI no: ]
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PubMed id
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Figure 1.
Fig, 1 Dependence of r -) on equilibrium concentration of
reagents ([Mb*] + [N3-]; see Eqn, 1), as obtained by temperature
ump experiments at 25°C, for N~- binding to the His(ET)Va/and
HisfET)Val.Th(ElO)Arg mutants of sperm whale Mb (panel A and
panel B, respectively). Dependence of the apparent rate constant
(kob,) on the concentration of reagents ([Mb ÷] - [N~-]), as obtained
by stopped-flow experiments at 20°C, for N~- binding to and
wild-type whale Mb's (panel ; circles and squares, respective-
ly), Straigl~t lines are linear regressions of data points. Data were ob-
tained at Mb concentration = 4.0 × 10 -6 M in 0,1 M phosphae buffer,
pH 7.0.
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Figure 2.
Fig. 2. Stereo view of the distal site environment, seen from the solvent side of the His(E7)VaI-Thr(ElO)Arg double mutant of sperm whale Mb
as model-built on he crystal structure of the sperm whale Mb:Na- adduct, refined at 1.9 ,~, resolution (M, Bolognesi, personal communication).
The E helix is on the right end side of the picture; the N3- molecule is shown between the home and the side chain of Arg ~7 (El0),
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The above figures are
reproduced from the cited reference
with permission from the Federation of European Biochemical Societies
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Secondary reference #2
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Title
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Binding mode of azide to ferric aplysia limacina myoglobin. Crystallographic analysis at 1.9 a resolution.
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Authors
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A.Mattevi,
G.Gatti,
A.Coda,
M.Rizzi,
P.Ascenzi,
M.Brunori,
M.Bolognesi.
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Ref.
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J Mol Recognit, 1991,
4,
1-6.
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PubMed id
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