1h98: Difference between revisions

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[[Image:1h98.gif|left|200px]]
{{Seed}}
[[Image:1h98.png|left|200px]]


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{{STRUCTURE_1h98|  PDB=1h98  |  SCENE=  }}  
{{STRUCTURE_1h98|  PDB=1h98  |  SCENE=  }}  


'''NEW INSIGHTS INTO THERMOSTABILITY OF BACTERIAL FERREDOXINS: HIGH RESOLUTION CRYSTAL STRUCTURE OF THE SEVEN-IRON FERREDOXIN FROM THERMUS THERMOPHILUS'''
===NEW INSIGHTS INTO THERMOSTABILITY OF BACTERIAL FERREDOXINS: HIGH RESOLUTION CRYSTAL STRUCTURE OF THE SEVEN-IRON FERREDOXIN FROM THERMUS THERMOPHILUS===




==Overview==
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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.
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{{ABSTRACT_PUBMED_11681700}}


==About this Structure==
==About this Structure==
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[[Category: Stability]]
[[Category: Stability]]
[[Category: Thermophilic]]
[[Category: Thermophilic]]
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