3hip
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HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM PURPURATUM
OverviewOverview
The crystal structure of the high-potential iron-sulfur protein (HiPIP), isolated from Chromatium purpuratum is reported at 2.7 A 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 approximately 175 degrees 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 approximately 13.0 A. 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.
About this StructureAbout this Structure
3HIP is a Single protein structure of sequence from Marichromatium purpuratum with SF4 as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure and possible dimerization of the high-potential iron-sulfur protein from Chromatium purpuratum., Kerfeld CA, Salmeen AE, Yeates TO, Biochemistry. 1998 Oct 6;37(40):13911-7. PMID:9760225
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