1CFM

CYTOCHROME F FROM CHLAMYDOMONAS REINHARDTII

Summary for 1CFM

• Entry DOI: 10.2210/pdb1cfm/pdb
• Descriptor: CYTOCHROME F, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: cytochrome f, plastocyanin, proton wire, heme, electron transport
• Biological source: Chlamydomonas reinhardtii
• Cellular location: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein: P23577
• Total number of polymer chains: 3
• Total formula weight: 83395.34

Authors

Chi, Y.I.,Huang, L.S.,Zhang, Z.,Fernandez-Velasco, J.G.,Malkin, R.,Berry, E.A. (deposition date: 1998-09-18, release date: 1999-04-27, Last modification date: 2024-10-23)

Primary citation

Chi, Y.I.,Huang, L.S.,Zhang, Z.,Fernandez-Velasco, J.G.,Berry, E.A.
X-ray structure of a truncated form of cytochrome f from chlamydomonas reinhardtii.
Biochemistry, 39:7689-7701, 2000

PubMed 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.

PubMed: 10869174
DOI: 10.1021/bi000090k

Experimental method

X-RAY DIFFRACTION (2 Å)