A truncated form of cytochrome
f from
Chlamydomonas reinhardtii (an important eukaryoticmodel organism for photosynthetic electron transfer studies) has been crystal
lized (space group
P2
12
12
1;three molecules/asymmetric unit) and its structure determined to 2.0 Å resolution by molecular replacementusing the coordinates of a truncated turnip cytochrome
f as a model. The structure displays the samefolding and detailed features as turnip cytochrome
f, including (a) an unusual heme Fe
ligation by the
-amino group of tyrosine 1, (b) a cluster of lysine residues (proposed docking site of plastocyanin), and(c) the presence of a chain of seven water molecules bound to conserved residues and extending betweenthe heme pocket and K58 and K66 at the lysine cluster. For this array of waters, we propose a structuralrole. Two cytochrome
f molecules are related by a noncrystallographic symmetry operator which is adistorted proper 2-fold rotation. This may represent the dimeric relation of the monomers in situ; however,the heme orientation suggested by this model is not consistent with previous EPR measurements on orientedmembranes.