1l5p
From Proteopedia
Crystal Structure of Trichomonas vaginalis Ferredoxin
Overview
Crystallographic studies revealing the three-dimensional structure of the oxidized form of the [2Fe-2S] ferredoxin from Trichomonas vaginalis (TvFd) are presented. TvFd, a member of the hydrogenosomal class of ferredoxins, possesses a unique combination of redox and spectroscopic properties, and is believed to be the biological molecule that activates the drug metronidazole reductively in the treatment of trichomoniasis. It is the first hydrogenosomal ferredoxin to have its structure determined. The structure of TvFd reveals a monomeric, 93 residue protein with a fold similar to that of other known [2Fe-2S] ferredoxins. It contains nine hydrogen bonds to the sulfur atoms of the cluster, which is more than the number predicted on the basis of the spectroscopic data. The TvFd structure contains a large dipole moment like adrenodoxin, and appears to have a similar interaction domain. Our analysis demonstrates that TvFd has a unique cavity near the iron-sulfur cluster that exposes one of the inorganic sulfur atoms of the cluster to solvent. This cavity is not seen in any other [2Fe-2S] ferredoxin with known structure, and is hypothesized to be responsible for the high rate of metronidazole reduction by TvFd.
About this Structure
1L5P is a Single protein structure of sequence from Trichomonas vaginalis. Full crystallographic information is available from OCA.
Reference
The crystal structure of Trichomonas vaginalis ferredoxin provides insight into metronidazole activation., Crossnoe CR, Germanas JP, LeMagueres P, Mustata G, Krause KL, J Mol Biol. 2002 Apr 26;318(2):503-18. PMID:12051855 Page seeded by OCA on Fri May 2 23:34:11 2008
