1jro
From Proteopedia
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Crystal Structure of Xanthine Dehydrogenase from Rhodobacter capsulatus
Overview
Xanthine dehydrogenase (XDH), a complex molybdo/iron-sulfur/flavoprotein, catalyzes the oxidation of hypoxanthine to xanthine followed by oxidation, of xanthine to uric acid with concomitant reduction of NAD+. The 2.7 A, resolution structure of Rhodobacter capsulatus XDH reveals that the, bacterial and bovine XDH have highly similar folds despite differences in, subunit composition. The NAD+ binding pocket of the bacterial XDH, resembles that of the dehydrogenase form of the bovine enzyme rather than, that of the oxidase form, which reduces O(2) instead of NAD+. The drug, allopurinol is used to treat XDH-catalyzed uric acid build-up occurring in, gout or during cancer chemotherapy. As a hypoxanthine analog, it is, oxidized to alloxanthine, which cannot be further oxidized but acts as a, tight binding inhibitor of XDH. The 3.0 A resolution structure of the, XDH-alloxanthine complex shows direct coordination of alloxanthine to the, molybdenum via a nitrogen atom. These results provide a starting point for, the rational design of new XDH inhibitors.
About this Structure
1JRO is a Protein complex structure of sequences from Rhodobacter capsulatus with CA, FES, MPN, MOS and FAD as ligands. Active as Xanthine dehydrogenase, with EC number 1.17.1.4 Full crystallographic information is available from OCA.
Reference
Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus., Truglio JJ, Theis K, Leimkuhler S, Rappa R, Rajagopalan KV, Kisker C, Structure. 2002 Jan;10(1):115-25. PMID:11796116
Page seeded by OCA on Sun Nov 25 00:07:07 2007
