Abstract:
:Detailed structural models of di-cluster seven-iron ferredoxins constitute a valuable resource for folding and stability studies relating the metal cofactors' role in protein stability. The here reported, hemihedric twinned crystal structure at 2.0 A resolution from Acidianus ambivalens ferredoxin, shows an integral 103 residues, physiologically relevant native form composed by a N-terminal extension comprising a His/Asp Zn(2+) site and the ferredoxin (betaalphabeta)(2) core, which harbours intact clusters I and II, a [3Fe-4S](1+/0) and a [4Fe-4S](2+/1+) centres. This is in contrast with the previously available ferredoxin structure from Sulfolofus tokodai, which was obtained from an artificial oxidative conversion with two [3Fe-4S](1+/0) centres and poor definition around cluster II.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Frazão C,Aragão D,Coelho R,Leal SS,Gomes CM,Teixeira M,Carrondo MAdoi
10.1016/j.febslet.2008.01.041subject
Has Abstractpub_date
2008-03-05 00:00:00pages
763-7issue
5eissn
0014-5793issn
1873-3468pii
S0014-5793(08)00066-5journal_volume
582pub_type
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