PDBsum entry 1plc

Electron transport

PDB id: 1plc

Contents

Protein chain

99 a.a.

Metals

_CU

Waters ×110

References listed in PDB file

Key reference

Title

Accuracy and precision in protein structure analysis: restrained least-Squares refinement of the structure of poplar plastocyanin at 1.33 a resolution.

Authors

J.M.Guss, H.D.Bartunik, H.C.Freeman.

Ref.

Acta Crystallogr B, 1992, 48, 790-811.

PubMed id

1492962

Abstract

The structure of the electron-transfer protein, plastocyanin (99 amino acids, one Cu atom, 10,500 Da) from poplar leaves, has been refined at 1.33 A resolution to a residual R = 0.15. The space group is orthorhombic, P2(1)2(1)2(1), a = 29.60 (1), b = 46.86 (3), c = 57.60 (3) A. The 14,303 reflections used in the refinement were obtained from a data set recorded on a four-circle diffractometer with radiation from a sealed fine-focus tube, combined with a data set measured on oscillation films exposed at the DESY synchrotron. The final model comprises 1442 (738 non-H) protein atoms, one Cu atom and 110 solvent molecules. Nine residues are described as disordered. The root-mean-square deviation from ideal bond lengths is 0.016 A and the root-mean-square difference between the positions of the C alpha atoms in this refined model and in the structure previously refined at 1.6 A resolution is 0.11 A. The effects of manual model adjustment, resolution, choice of standard values for geometrical parameters, inclusion of H atoms and inclusion of anomalous-scattering corrections on the copper-site geometry have been explored. The final values of the Cu-ligand bond lengths are: Cu--N(His37) 1.91, Cu--S(Cys84) 2.07, Cu--N(His87) 2.06, Cu--S(Met92) 2.82 A.

Secondary reference #1

Title

Structure of oxidized poplar plastocyanin at 1.6 a resolution.

Authors

J.M.Guss, H.C.Freeman.

Ref.

J Mol Biol, 1983, 169, 521-563. [DOI no: 10.1016/S0022-2836(83)80064-3]

PubMed id

6620385

Figure 7.
Fro. 7. Stereo view of the Cu site in Cu-plastocyanin. All on-hydrogen atoms of each ligand residue (N, C~. C, O, side-chain) are shown.

Figure 13.
Fro. 13. The same stereo view of the plastocyanin molecule as in Fig. II, but emphasizing acidic residues that are invariant or conservatively substituted in plant lstocyanins. Residues shown with black side-chains are Glu25, Asp42, Glu43, Asp44, Set45 (Glu n most other plastoeyanins), AspS1, Glu59, Asp61 and Glu68. In ddition, Tyr83 nd Gin88 (which are invariant in plant plastocyanins) am included but not dluwn in lack.

The above figures are reproduced from the cited reference with permission from Elsevier

Secondary reference #2

Title

X-Ray crystal structure analysis of plastocyanin at 2.7 angstroms resolution

Authors

P.M.Colman, H.C.Freeman, J.M.Guss, M.Murata, V.A.Norris, J.A.M.Ramshaw, M.P.Venkatappa.

Ref.

nature, 1978, 272, 319.

Secondary reference #3

Title

Preliminary crystallographic data for a copper-Containing protein, Plastocyanin.

Authors

G.V.Chapman, P.M.Colman, H.C.Freeman, J.M.Guss, M.Murata, V.A.Norris, J.A.Ramshaw, M.P.Venkatappa.

Ref.

J Mol Biol, 1977, 110, 187-189. [DOI no: 10.1016/S0022-2836(77)80106-X]

PubMed id

845945

Figure 1.
Fro. 1. An 1~ ~ precesion photograph of the hOl zone of poplar plastocyanin. Exposure time was 40 h in Ni-filtered Cu radiaton from a sealed tubeoperating at 40 kV and 20 mA.

The above figure is reproduced from the cited reference with permission from Elsevier