The β sheet is folded in such a way that the strands at the front and the back of the shell are roughly perpendicular to each other (Fig. 1b). The opening in the shell is situated toward the center of the trimer, forming the shape of a shell. The six α-helices are located at the open end of the shell and mainly connect the separated β-strands. BChl a molecules 1 and 2 are situated at the outside of the protein complex, selleck while BChl a 3–7 are located in the center

(Fig. 1c). Polar interactions and salt bridges between amino acids insure the formation of a stable trimer. The magnesium ion is a five-coordinate in all the BChl a molecules, although the fifth ligand varies between the pigments. For BChl a 1, 3, 4, 6, and 7, it is a histidine residue, for BChl a 5, it is an oxygen atom from a leucine residue, and for BChl a 2, the electron density suggests a water molecule as the fifth ligand. The structures of

the FMO AZD1152-HQPA molecular weight protein present in the two species Prosthecochloris aestuarii and Chlorobium tepidum show a high degree of similarity (the amino acid sequences are identical to one another within 77%). The residues that are not conserved do not alter the interaction between the protein and the BChl a molecules. Besides that, the relative positions of each of the BChl a molecules in the two species match almost perfectly. The main difference is in the planarity of the tetrapyrrole ring of the BChl a molecules. For a more detailed description of the comparison between the two species, see Li et al. (1997) and the discussion at the end of this section. Various spectroscopic investigations using linear absorption spectroscopy, circular dichroism (CD) and linear dichroism (LD) on samples of the isolated FMO protein and the protein associated with membrane vesicles have revealed the orientation of the proteins with respect to the membrane (Melkozernov et al. 1998). The three subunits of the FMO protein are related by C 3 symmetry and can be modeled as Oxalosuccinic acid disks, with the axis of the disks parallel to the C 3 axis (Fig. 2a). The spectroscopic studies show that the C 3 symmetry axis of the three subunits of the FMO protein

is perpendicular to the membrane plane. This implies that the flat sides of the discs is embedded in the membrane (Fig. 2a). Fig. 2 Orientation of the FMO protein. a The C 3 axis that relates the three subunits of the FMO protein is parallel to the disc axis and perpendicular to the membrane plane. b The angles between the Q y transitions of the seven BChl a pigments with respect to the C 3 axis (Iseri and Gülen 1999) In two recent studies, the presence of an additional BChl a molecule per monomer was proposed. This observation is based on careful studies of high resolution X-ray data. Ben-Shem et al. noticed additional electron density at the interface between the monomers in their newly crystalized and solved structure.