3HIP
HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM PURPURATUM
Summary for 3HIP
| Entry DOI | 10.2210/pdb3hip/pdb |
| Descriptor | HIGH-POTENTIAL IRON-SULFUR PROTEIN, IRON/SULFUR CLUSTER (2 entities in total) |
| Functional Keywords | electron transfer, photosynthesis, metalloprotein |
| Biological source | Marichromatium purpuratum |
| Cellular location | Periplasm: P59860 |
| Total number of polymer chains | 3 |
| Total formula weight | 27340.28 |
| Authors | Kerfeld, C.A.,Salmeen, A.E.,Yeates, T.O. (deposition date: 1998-06-15, release date: 1998-11-11, Last modification date: 2024-05-22) |
| Primary citation | Kerfeld, C.A.,Salmeen, A.E.,Yeates, T.O. Crystal structure and possible dimerization of the high-potential iron-sulfur protein from Chromatium purpuratum. Biochemistry, 37:13911-13917, 1998 Cited by PubMed Abstract: 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. PubMed: 9760225DOI: 10.1021/bi9810252 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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