The Role of System-Specific Molecular Chaperones in the Maturation of Molybdoenzymes in Bacteria
Figure 2
Overall structure and cofactor arrangement of R. capsulatus XDH. R. capsulatus XDH forms an (αβ)2 heterotetramer. The XdhA subunits are drawn in light green and light blue and the XdhB subunits in dark green and dark blue. The [2Fe-2S] and FAD cofactors of XdhA and the Moco of XdhB are shown as space-filling models. The Moco is deeply buried in the XdhB subunit being only accessible through a substrate-binding channel. Also shown is the coordination of Moco and FeSI, FeSII and FAD at the active site of R. capsulatus XDH and the reaction catalyzed by XDH. The structures were generated using the coordinates from the Protein Data Bank (accession number 1JRO).
