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1h98
From Proteopedia
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Revision as of 13:27, 30 October 2007
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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 ... [(full description)]
About this Structure
1H98 is a [Single protein] structure of sequence from [Thermus aquaticus] with SF4 and F3S as [ligands]. Structure known Active Site: FS4. 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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