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PDBsum entry 1id2
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Electron transport
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PDB id
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1id2
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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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Crystal structure analysis and refinement at 2.15 a resolution of amicyanin, A type i blue copper protein, From thiobacillus versutus.
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Authors
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A.Romero,
H.Nar,
R.Huber,
A.Messerschmidt,
A.P.Kalverda,
G.W.Canters,
R.Durley,
F.S.Mathews.
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Ref.
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J Mol Biol, 1994,
236,
1196-1211.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of the type I blue copper protein amicyanin from
Thiobacillus versutus has been determined by Patterson search techniques on the
basis of the molecular model of amicyanin from Paracoccus denitrificans, and
refined by energy-restrained least-squares methods. Amicyanin crystallizes in
the trigonal space group P3(2) with unit cell dimensions of a = b = 87.40 A, c =
38.20 A. The asymmetric unit is composed of three independent molecules centred
on the crystallographic 3(2) axes. The final R-value is 17.4% for 15,984
reflections to a resolution of 2.15 A. The polypeptide fold in amicyanin is
based on the beta-sandwich structure commonly found in blue copper proteins.
Nine beta strands are folded into two twisted beta-sheets that pack together
with a filling of non-polar residues between them. The geometry of the copper
site is similar to that of plastocyanin. There are four ligands, arranged
approximately as a distorted tetrahedron, to the copper atom: His54, Cys93,
His96 and Met99. One of the copper ligands, His96, is exposed to the surface and
lies in the centre of a cluster of seven hydrophobic residues.
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Figure 3.
Figure 3. A section (z= 14/42) of the difference Patterson map compute at 3.5 A resolution. Two sites relaed by
translation of z, ) = (2/3, l/3) g' Ives rse to identical position in the difference Patterson map which in turn explains the
elative peak heights of 2 : I or the 2 Harker peaks.
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Figure 8.
Fgure 8. C:rvstal acking of amicyanin from T. versrt&. The 3 independent molecules of amicyanin are arranged as
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(1994,
236,
1196-1211)
copyright 1994.
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