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X-ray structure of a truncated form of cytochrome f from chlamydomonas reinhardtii. Biochemistry 2000 Jul 04;39(26):7689-701

Date

06/28/2000

Pubmed ID

10869174

DOI

10.1021/bi000090k

Scopus ID

2-s2.0-0034604237   45 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 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.

Author List

Chi YI, Huang LS, Zhang Z, Fernández-Velasco JG, Berry EA

Author

Young-In Chi PhD Assistant Professor in the Surgery department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Amino Acid Sequence
Animals
Chlamydomonas reinhardtii
Crystallography, X-Ray
Cytochromes
Cytochromes f
Dimerization
Heme
Lysine
Models, Molecular
Molecular Sequence Data
Protein Conformation
Sequence Homology, Amino Acid