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Crystallization (Commentary)
Reference
1.1.9.1
to 1.44 A resolution. The N-terminal domain has a beta-propeller fold and binds one pyrroloquinoline quinone cofactor and one calcium ion in the active site. A tetrahydrofuran-2-carboxylic acid molecule is present in the substrate-binding cleft. The C-terminal domain is an -helical type I cytochrome c with His608 and Met647 as heme-iron ligands. An unusual disulfide bond between two adjacent cysteines bridges the redox centers. It appears essential for electron transfer. A water channel delineates a possible pathway for proton transfer from the active site to the solvent
656080
1.1.9.1
to 2.4 A resolution, space group C2
701480
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