2pcy
From Proteopedia
(New page: 200px<br /><applet load="2pcy" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pcy, resolution 1.8Å" /> '''THE CRYSTAL STRUCTURE...) |
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| - | [[Image:2pcy.gif|left|200px]]<br /><applet load="2pcy" size=" | + | [[Image:2pcy.gif|left|200px]]<br /><applet load="2pcy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2pcy, resolution 1.8Å" /> | caption="2pcy, resolution 1.8Å" /> | ||
'''THE CRYSTAL STRUCTURE OF POPLAR APOPLASTOCYANIN AT 1.8-ANGSTROMS RESOLUTION. THE GEOMETRY OF THE COPPER-BINDING SITE IS CREATED BY THE POLYPEPTIDE'''<br /> | '''THE CRYSTAL STRUCTURE OF POPLAR APOPLASTOCYANIN AT 1.8-ANGSTROMS RESOLUTION. THE GEOMETRY OF THE COPPER-BINDING SITE IS CREATED BY THE POLYPEPTIDE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of apoplastocyanin from poplar leaves | + | The three-dimensional structure of apoplastocyanin from poplar leaves (Populus nigra var. italica) has been determined by x-ray diffraction at 1.8-A resolution. The structure closely resembles that of the holoprotein. In particular, the positions of the copper-binding residues in the apo- and holoproteins differ by only 0.1-0.3 A. This indicates that the irregular geometry of the "type 1" copper site is imposed upon the metal atom by the polypeptide moiety. A 180 degrees rotation of one solvent-exposed histidine imidazole ring about C beta-C gamma appears to facilitate access to the copper site. The close structural similarity between apo-, Cu-(II)-, and Cu(I)-plastocyanin was initially demonstrated by means of electron density difference maps. Two series of restrained least squares refinement calculations for apoplastocyanin, originating from different sets of atomic positional parameters, were carried out in parallel. Both refinements converged to the same model which, when fully refined, had a residual R = 0.16. Forty-two water molecules were located during the refinement. |
==About this Structure== | ==About this Structure== | ||
| - | 2PCY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Populus_nigra Populus nigra]. Full crystallographic information is available from [http:// | + | 2PCY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Populus_nigra Populus nigra]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PCY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Populus nigra]] | [[Category: Populus nigra]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Freeman, H | + | [[Category: Freeman, H C.]] |
| - | [[Category: Garrett, T | + | [[Category: Garrett, T P.J.]] |
| - | [[Category: Guss, J | + | [[Category: Guss, J M.]] |
[[Category: electron transport protein(cuproprotein)]] | [[Category: electron transport protein(cuproprotein)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:28:18 2008'' |
Revision as of 16:28, 21 February 2008
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THE CRYSTAL STRUCTURE OF POPLAR APOPLASTOCYANIN AT 1.8-ANGSTROMS RESOLUTION. THE GEOMETRY OF THE COPPER-BINDING SITE IS CREATED BY THE POLYPEPTIDE
Overview
The three-dimensional structure of apoplastocyanin from poplar leaves (Populus nigra var. italica) has been determined by x-ray diffraction at 1.8-A resolution. The structure closely resembles that of the holoprotein. In particular, the positions of the copper-binding residues in the apo- and holoproteins differ by only 0.1-0.3 A. This indicates that the irregular geometry of the "type 1" copper site is imposed upon the metal atom by the polypeptide moiety. A 180 degrees rotation of one solvent-exposed histidine imidazole ring about C beta-C gamma appears to facilitate access to the copper site. The close structural similarity between apo-, Cu-(II)-, and Cu(I)-plastocyanin was initially demonstrated by means of electron density difference maps. Two series of restrained least squares refinement calculations for apoplastocyanin, originating from different sets of atomic positional parameters, were carried out in parallel. Both refinements converged to the same model which, when fully refined, had a residual R = 0.16. Forty-two water molecules were located during the refinement.
About this Structure
2PCY is a Single protein structure of sequence from Populus nigra. Full crystallographic information is available from OCA.
Reference
The crystal structure of poplar apoplastocyanin at 1.8-A resolution. The geometry of the copper-binding site is created by the polypeptide., Garrett TP, Clingeleffer DJ, Guss JM, Rogers SJ, Freeman HC, J Biol Chem. 1984 Mar 10;259(5):2822-5. PMID:6698995
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