1L5P

Crystal Structure of Trichomonas vaginalis Ferredoxin

Summary for 1L5P

• Entry DOI: 10.2210/pdb1l5p/pdb
• Descriptor: ferredoxin, FE2/S2 (INORGANIC) CLUSTER (3 entities in total)
• Functional Keywords: [2fe-2s] cluster, electron transfer, iron-sulfur protein, metalloprotein, oxidoreductase
• Biological source: Trichomonas vaginalis
• Cellular location: Hydrogenosome: P21149
• Total number of polymer chains: 3
• Total formula weight: 29903.48

Authors

Crossnoe, C.R.,Germanas, J.P.,Le Magueres, P.,Mustata, G.,Krause, K.L. (deposition date: 2002-03-07, release date: 2002-08-21, Last modification date: 2024-02-14)

Primary citation

Crossnoe, C.R.,Germanas, J.P.,LeMagueres, P.,Mustata, G.,Krause, K.L.
The crystal structure of Trichomonas vaginalis ferredoxin provides insight into metronidazole activation.
J.Mol.Biol., 318:503-518, 2002

PubMed Abstract: 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.

PubMed: 12051855
DOI: 10.1016/S0022-2836(02)00051-7

Experimental method

X-RAY DIFFRACTION (2.2 Å)