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PDBsum entry 2gim
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Electron transport
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PDB id
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2gim
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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 of plastocyanin from the cyanobacterium anabaena variabilis.
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Authors
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L.Schmidt,
H.E.Christensen,
P.Harris.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2006,
62,
1022-1029.
[DOI no: ]
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PubMed id
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Abstract
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Plastocyanin from the cyanobacterium Anabaena variabilis was heterologously
produced in Escherichia coli and purified. Plate-like crystals were obtained by
crystallization in 1.15 M trisodium citrate and 7.67 mM sodium borate buffer pH
8.5. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with
unit-cell parameters a = 67.85, b = 45.81, c = 63.41 Angstrom. The structure of
the oxidized protein was solved to a resolution of 1.6 Angstrom using
plastocyanin from Phormidium laminosum as a search model. Two molecules were
found in the asymmetric unit. The electrostatic surface of the basic protein
showed a large population of positively charged residues in the northern site,
whereas the eastern site lacked the two strongly negatively charged patches. The
copper ion was found to be relatively mobile and there were two distinct
conformations of His61.
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Figure 2.
Figure 2 Superimposed structures of A. variabilis plastocyanin
(red and cyan) and poplar plastocyanin (green and grey; PDB code
1plc ; Guss et al., 1992[Guss, J. M., Bartunik, H. D. & Freeman,
H. C. (1992). Acta Cryst. B48, 790-811.]). The structures are
represented by the C^  atoms
and the Cu ions. 58-61 refer to the residues Ser58-Asp61 in
poplar plastocyanin. The figure was prepared using CCP4mg
(Potterton et al., 2002[Potterton, E., McNicholas, S.,
Krissinel, E., Cowtan, K. & Noble, M. (2002). Acta Cryst. D58,
1955-1957.]).
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Figure 5.
Figure 5 2F[obs] - F[calc]  [A]-weighted
electron-density map showing the hydrogen-bonding networks of
the two conformations of His61 in A. variabilis chains A (left)
and C (right). The higher occupied (occupancy 0.55 in chain A
and 0.65 in chain C) conformations are shown in green (C-atom
colour) and the lower occupied (0.45 in chain A and 0.35 in
chain C) are shown in light blue. This figure was produced using
PyMOL (DeLano, 2002[DeLano, W. L. (2002). The PyMOL Molecular
Visualization System. DeLano Scientific, San Carlos, CA, USA.
http://www.pymol.org .]).
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2006,
62,
1022-1029)
copyright 2006.
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