1cfm
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CYTOCHROME F FROM CHLAMYDOMONAS REINHARDTII
OverviewOverview
A truncated form of cytochrome f from Chlamydomonas reinhardtii (an, important eukaryotic model organism for photosynthetic electron transfer, studies) has been crystallized (space group P2(1)2(1)2(1); three, molecules/asymmetric unit) and its structure determined to 2.0 A, 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 alpha-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.
About this StructureAbout this Structure
1CFM is a Single protein structure of sequence from Chlamydomonas reinhardtii with HEM as ligand. Full crystallographic information is available from OCA.
ReferenceReference
X-ray structure of a truncated form of cytochrome f from chlamydomonas reinhardtii., Chi YI, Huang LS, Zhang Z, Fernandez-Velasco JG, Berry EA, Biochemistry. 2000 Jul 4;39(26):7689-701. PMID:10869174
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