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Title
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Crystal structure of myoglobin from a synthetic gene.
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Authors
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G.N.Phillips,
R.M.Arduini,
B.A.Springer,
S.G.Sligar.
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Ref.
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Proteins, 1990,
7,
358-365.
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PubMed id
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Abstract
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Crystals have been grown of myoglobin produced in Escherichia coli from a
synthetic gene, and the structure has been solved to 1.9 A resolution. The space
group of the crystals is P6, which is different from previously solved myoglobin
crystal forms. The synthetic myoglobin is essentially identical to myoglobin
isolated from sperm whale tissue, except for the retention of the initiator
methionine at the N-terminus and the substitution of asparagine for aspartic
acid at position 122. Superposition of the coordinates of native and synthetic
sperm whale myoglobins reveals only minor changes in the positions of main chain
atoms and reorientation of some surface side chains. Crystals of variants of the
"synthetic" myoglobin have also been grown for structural analysis of the role
of key amino acid residues in ligand binding and specificity.
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