1h98
From Proteopedia
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NEW INSIGHTS INTO THERMOSTABILITY OF BACTERIAL FERREDOXINS: HIGH RESOLUTION CRYSTAL STRUCTURE OF THE SEVEN-IRON FERREDOXIN FROM THERMUS THERMOPHILUS
Overview
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.
About this Structure
1H98 is a Single protein structure of sequence from Thermus aquaticus with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
New insights into the thermostability of bacterial ferredoxins: high-resolution crystal structure of the seven-iron ferredoxin from Thermus thermophilus., Macedo-Ribeiro S, Martins BM, Pereira PJ, Buse G, Huber R, Soulimane T, J Biol Inorg Chem. 2001 Sep;6(7):663-74. PMID:11681700
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