X-ray Structure of a Truncated Form of Cytochrome f from Chlamydomonas reinhardtii†,‡
journal contributionposted on 06.06.2000, 00:00 by Young-In Chi, Li-Shar Huang, Zhaolei Zhang, Javier G. Fernández-Velasco, Edward A. Berry
A truncated form of cytochrome f from Chlamydomonas reinhardtii (an important eukaryotic model organism for photosynthetic electron transfer studies) has been crystallized (space group P212121; three molecules/asymmetric unit) and its structure determined to 2.0 Å resolution by molecular replacement using the coordinates of a truncated turnip cytochrome f as a model. The structure displays the same folding and detailed features as turnip cytochrome f, including (a) an unusual heme Fe ligation by the α-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 between the heme pocket and K58 and K66 at the lysine cluster. For this array of waters, we propose a structural role. Two cytochrome f molecules are related by a noncrystallographic symmetry operator which is a distorted 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 oriented membranes.
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eukaryotic model organismphotosynthetic electron transfer studiesdimeric relationcytochrome f moleculesChlamydomonas reinhardtiiheme pocketwater moleculesheme Fe ligation2.0 Å resolutionlysine clusterlysine residuesCytochrome fdocking siteturnip cytochrome fEPR measurementsK 66space group P 2 1 2 1 2 1noncrystallographic symmetry operatorheme orientationTruncated Formcytochrome fK 58structure displays