1H98
New Insights into Thermostability of Bacterial Ferredoxins: High Resolution Crystal Structure of the Seven-Iron Ferredoxin from Thermus thermophilus
Summary for 1H98
| Entry DOI | 10.2210/pdb1h98/pdb |
| Descriptor | FERREDOXIN, IRON/SULFUR CLUSTER, FE3-S4 CLUSTER, ... (4 entities in total) |
| Functional Keywords | electron transport, thermophilic, iron-sulfur, azotobacter, hydrogen bonds, stability, high resolution |
| Biological source | THERMUS AQUATICUS |
| Total number of polymer chains | 1 |
| Total formula weight | 9341.30 |
| Authors | Macedo-Ribeiro, S.,Martins, B.M.,Pereira, P.J.B.,Buse, G.,Huber, R.,Soulimane, T. (deposition date: 2001-03-05, release date: 2001-11-27, Last modification date: 2023-12-13) |
| Primary citation | Macedo-Ribeiro, S.,Martins, B.M.,Pereira, P.J.B.,Buse, G.,Huber, R.,Soulimane, T. New Insights Into the Thermostability of Bacterial Ferredoxins: High-Resolution Crystal Structure of the Seven-Iron Ferredoxin from Thermus Thermophilus J.Biol.Inorg.Chem., 6:663-, 2001 Cited by PubMed Abstract: The crystal structure of the seven-iron ferredoxin from Thermus thermophilus (FdTt) has been determined at 1.64 A resolution, allowing us to unveil the common mechanisms of thermostabilization within "bacterial-type" ferredoxins. FdTt and other homologous thermophilic seven-iron ferredoxins are smaller than their mesophilic counterparts. Thermostabilizing features are optimized in a minimal structural and functional unit, with an extensive cross-linking of secondary structure elements mediated by improved polar and hydrophobic interactions. Most of the potentially stabilizing features are focused on the vicinity of the functional [3Fe-4S] cluster. The structural [4Fe-4S] cluster is shielded in thermophilic FdTt by an increased number of polar interactions involving the two N-terminal residues. Comparisons with the hyperthermostable ferredoxin from Thermotoga maritima reveal that (1) a reduction in the number of non-glycine residues in strained conformations, (2) improved polar interactions within the common iron-sulfur cluster binding (betaalphabeta)2 motif, and (3) an optimized charge distribution at the protein surface, constitute a common strategy for increasing the thermal stability of these ferredoxins. PubMed: 11681700DOI: 10.1007/S007750100243 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.64 Å) |
Structure validation
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