Three-dimensional structure of higher plant photosystem I determined by electron crystallography.
We describe the three-dimensional structure of higher plant photosystem I (PSI) as obtained by electron microscopy of two-dimensional crystals formed at the grana margins of thylakoid membranes. The negatively stained crystalline areas displayed unit cell dimensions a = 26.6 nm, b = 27.7 nm, and gamma = 90(o), and p22121 plane group symmetry consisting of two monomers facing upward and two monomers facing downward with respect to the membrane plane. Higher plant PSI shows several structural similarities to the cyanobacterial PSI complex, with a prominent ridge on the stromal side of the complex. The stromal ridge is resolved into at least three separate domains that are interpreted as representing the three well characterized stromal subunits, the psa C, D, and E gene products. The lumenal surface is relatively flat but exhibits a distinct central depression that may be the binding site for plastocyanin. Higher plant PSI is of dimensions 15-16 x 11-12.5 nm, and thus leaves a larger footprint in the membrane than its cyanobacterial equivalent (13 x 10.5 nm). It is expected that additional membrane-bound polypeptides will be present in the higher plant PSI. Both higher plant and cyanobacterial complexes span about 8-9 nm in the direction orthogonal to the membrane. This report represents the first three-dimensional structure for the higher plant PSI complex.
Kitmitto
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A
Department of Biomolecular Sciences, UMIST, Manchester, M60 1QD, United Kingdom.
Mustafa
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AO
Holzenburg
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Ford
R C
RC
D003461:Crystallography; D008854:Microscopy, Electron; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000648:ultrastructure; D045331:Photosystem I Protein Complex; D011487:Protein Conformation; D018724:Spinacia oleracea / Q000737:chemistry*
D045322:Photosynthetic Reaction Center Complex Proteins; D045331:Photosystem I Protein Complex