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PDBsum entry 1bvc
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Oxygen storage
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PDB id
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1bvc
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References listed in PDB file
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Key reference
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Title
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Structure determination of the biliverdin apomyoglobin complex: crystal structure analysis of two crystal forms at 1.4 and 1.5 a resolution.
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Authors
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U.G.Wagner,
N.Müller,
W.Schmitzberger,
H.Falk,
C.Kratky.
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Ref.
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J Mol Biol, 1995,
247,
326-337.
[DOI no: ]
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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
96%.
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Abstract
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Crystal structure determinations of two orthorhombic (P2(1)2(1)2(1)) crystal
modifications of the biliverdin apomyoglobin complex are described. The two
structures were determined by X-ray diffraction at 100 K to a resolution of 1.5
A and 1.4 A. Both crystal forms were grown by hanging-drop techniques, using
phosphate as precipitant. The structures were solved by molecular replacement
and refined to final R-values of 19.4% and 21.2%. Both structures are very
similar with respect to the binding site and the conformation of the biliverdin
chromophore, which occurs in a (P) helical conformation. It is located within
the heme pocket, very close in position and orientation to the heme binding site
in myoglobin. Two water molecules not present in the crystal structure of
myoglobin are sequestered within the heme pocket in the biliverdin-apomyoglobin
complex, and they are engaged in hydrogen bonding to the biliverdin and to the
protein. Comparison with structural results from an earlier NMR study of the
same complex shows good agreement.
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Figure 4.
Figure 4. Schematic representations of the hydrogen
bonds involving the biliverdin molecule, the 2 water
molecules (WAT2 and WAT1) and the 2 histidine residues
(His93 and His64). The interatomic distances given in the
Figure are from the crystal structure of blv-Mb-D. The
corresponding distances from the crystal structure of
blv-Mb-B are as follows: N(His64). . .WAT1, 2.88;
WAT1. . .O(A), 2.66; N(B). . .N(His93), 2.95; O(B). . .WAT2,
2.79; WAT2. . .N(His93), 3.29 Å .
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Figure 8.
Figure 8. Two disordered residues in the blv-Mb-D
crystal structure. The spacial proximity of the 2 residues
creates a pair of mutually exclusive conformations in such
a way, that the conformation represented by full lines for
the one residue is incompatible with the conformation
represented by dotted lines for the other residue, and vice
versa.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(1995,
247,
326-337)
copyright 1995.
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Secondary reference #1
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Title
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Nuclear-Magnetic-Resonance investigations of the biliverdin-Apomyoglobin complex.
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Authors
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H.Marko,
N.Müller,
H.Falk.
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Ref.
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Eur J Biochem, 1990,
193,
573-580.
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PubMed id
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