Crystal Structure and Possible Dimerization of the High-Potential Iron−Sulfur Protein fromChromatiumpurpuratum,

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Abstract
The crystal structure of the high-potential iron−sulfur protein (HiPIP) isolated from Chromatium purpuratum is reported at 2.7 Å resolution. The three HiPIP molecules in the asymmetric unit of the crystals form one and one-half dimers. Two molecules are related by a noncrystallographic symmetry rotation of ∼175° with negligible translation along the dyad axis. The third molecule in the asymmetric unit also forms a dimer with a second HiPIP molecule across the crystallographic 2-fold symmetry axis. The Fe4S4 clusters in both the crystallographic and noncrystallographic dimers are separated by ∼13.0 Å. Solution studies give mixed results regarding the oligomeric state of the C. purpuratum HiPIP. A comparison with crystal structures of HiPIPs from other species shows that HiPIP tends to associate rather nonspecifically about a conserved, relatively hydrophobic surface patch to form dimers.

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