Download MendeleyCrystallographic analysis of the intact metal centres [3Fe-4S](1+/0) and [4Fe-4S](2+/1+) in a Zn(2+) -containing ferredoxin.
Frazao, C., Aragao, D., Coelho, R., Leal, S.S., Gomes, C.M., Teixeira, M., Carrondo, M.A.(2008) FEBS Lett 582: 763-767
- PubMed: 18258200
- DOI: https://doi.org/10.1016/j.febslet.2008.01.041
- Primary Citation of Related Structures:
2VKR - PubMed 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.
Organizational Affiliation:
Instituto Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av da República, Oeiras, Portugal. frazao@itqb.unl.pt
