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PDBsum entry 1myh
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Oxygen storage
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PDB id
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1myh
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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High-Resolution X-Ray structures of pig metmyoglobin and two cd3 mutants: mb(lys45----Arg) and mb(lys45----Ser).
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Authors
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T.J.Oldfield,
S.J.Smerdon,
Z.Dauter,
K.Petratos,
K.S.Wilson,
A.J.Wilkinson.
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Ref.
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Biochemistry, 1992,
31,
8732-8739.
[DOI no: ]
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PubMed id
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Abstract
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The structure of pig aquometmyoglobin has been refined to a crystallographic
R-factor of 19.8% against X-ray diffraction data between 10- and 1.75-A spacing.
The final structural model comprises two molecules of pig myoglobin, 233 water
molecules, and two sulfate ions. A water molecule is coordinated to each of the
heme iron atoms with an average Fe-OH2 bond distance of 2.19 A, and the mean
Fe-N epsilon (proximal histidine-93) distance is 2.20 A. In contrast to the
structure of sperm whale metmyoglobin, the iron is not significantly displaced
from the plane of the heme. At the entrance to the heme pocket, the side-chain
amino group of lysine-45 (CD3) is well-defined in the electron density map and
forms salt-bridging interactions with the heme 6-propionate and with a sulfate
ion. Serine and arginine replacements have been made previously at position 45
to examine the proposal that the CD3 side chain acts as a barrier to ligand
entry into the protein. Crystal structures of the arginine-45 and serine-45
mutant metmyoglobins have been solved to 1.9 and 2.0 A resolution, respectively.
In both cases the structural changes are confined to the site of mutation.
Arginine-45 takes up a conformation closely similar to that observed for this
residue in wild-type sperm whale myoglobin, in which it makes more extensive
charge-charge and charge-dipole interactions and appears to restrict the
movement of the distal histidine away from the ligand. The hydroxyl group of
serine-45 is disordered, but it is clear that the effect of the mutation is to
open up the solvent-exposed face of the heme pocket.
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Secondary reference #1
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Title
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Determination of the crystal structure of recombinant pig myoglobin by molecular replacement and its refinement.
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Authors
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S.J.Smerdon,
T.J.Oldfield,
E.J.Dodson,
G.G.Dodson,
R.E.Hubbard,
A.J.Wilkinson.
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Ref.
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Acta Crystallogr B, 1990,
46,
370-377.
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PubMed id
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Secondary reference #2
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Title
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Apomyoglobin as a molecular recognition surface: expression, Reconstitution and crystallization of recombinant porcine myoglobin in escherichia coli.
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Authors
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G.Dodson,
R.E.Hubbard,
T.J.Oldfield,
S.J.Smerdon,
A.J.Wilkinson.
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Ref.
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Protein Eng, 1988,
2,
233-237.
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PubMed id
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