X-ray structure of a truncated form of cytochrome f from Chlamydomonas reinhardtii

Chi Young-In, Li Shar Huang, Zhaolei Zhang, Javier G. Fernández-Velasco, Edward A. Berry

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44 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)7689-7701
Number of pages13
JournalBiochemistry
Volume39
Issue number26
DOIs
StatePublished - Jul 4 2000

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