3hip
HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM PURPURATUMHIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM PURPURATUM
Structural highlights
FunctionHIP_MARPU Specific class of high-redox-potential 4Fe-4S ferredoxins. Functions in anaerobic electron transport in most purple and in some other photosynthetic bacteria and in at least one genus (Paracoccus) of halophilic, denitrifying bacteria. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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