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PDBsum entry 1e67
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Electron transport
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PDB id
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1e67
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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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Characterization and crystal structure of zinc azurin, A by-Product of heterologous expression in escherichia coli of pseudomonas aeruginosa copper azurin.
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Authors
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H.Nar,
R.Huber,
A.Messerschmidt,
A.C.Filippou,
M.Barth,
M.Jaquinod,
M.Van de kamp,
G.W.Canters.
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Ref.
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Eur J Biochem, 1992,
205,
1123-1129.
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PubMed id
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Abstract
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Azurin*, a by-product of heterologous expression of the gene encoding the blue
copper protein azurin from Pseudomonas aeruginosa in Escherichia coli, was
characterized by chemical analysis and electrospray ionization mass
spectrometry, and its structure determined by X-ray crystallography. It was
shown that azurin* is native azurin with its copper atom replaced by zinc in the
metal binding site. Zinc is probably incorporated in the apo-protein after its
expression and transport into the periplasm. Holo-azurin can be reconstituted
from azurin* by prolonged exposure of the protein to high copper ion
concentrations or unfolding of the protein and refolding in the presence of
copper ions. An X-ray crystallographic analysis of azurin* at 0.21-nm resolution
revealed that the overall structure of azurin is not perturbed by the metal
exchange. However, the geometry of the co-ordination sphere changes from
trigonal bipyramidal in the case of copper azurin to distorted tetrahedral for
the zinc protein. The copper ligand Met121 is no longer co-ordinated to zinc
which adopts a position close to the carbonyl oxygen atom from residue Gly45.
The polypeptide structure surrounding the metal site undergoes moderate
reorganization upon zinc binding. The largest displacement observed is for the
carbonyl oxygen from residue Gly45, which is involved in copper and zinc
binding. It moves by 0.03 nm towards the zinc, thereby reducing its distance to
the metal from 0.29 nm in the copper protein to 0.23 nm in the derivative.
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Secondary reference #1
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Title
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Crystal structure analysis of oxidized pseudomonas aeruginosa azurin at ph 5.5 and ph 9.0. A ph-Induced conformational transition involves a peptide bond flip.
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Authors
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H.Nar,
A.Messerschmidt,
R.Huber,
M.Van de kamp,
G.W.Canters.
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Ref.
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J Mol Biol, 1991,
221,
765-772.
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PubMed id
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