3rp7

Crystal Structure of Klebsiella pneumoniae HpxO complexed with FAD and uric acid

spinqualitylabelsall models 3rp7, resolution 2.04Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3rp7 is a 1 chain structure with sequence from Klebsiella pneumoniae subsp. pneumoniae MGH 78578. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.042Å Ligands: FAD, MSE, URC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed HpxO is a flavin-dependent urate oxidase that catalyzes the hydroxylation of uric acid to 5-hydroxyisourate and functions in a novel pathway for purine catabolism found in Klebsiella pneumoniae. We have determined the structures of HpxO with and without uric acid at 2.0 A and 2.2 A, respectively. We have also determined the structure of the R204Q mutant at 2.0 A resolution in the absence of uric acid. The mutant structure is very similar to wild type HpxO except for the conformation of Arg103, which interacts with FAD in the mutant but not in the wild type structure. Interestingly, the R204Q mutation results in the uncoupling of NADH oxidation from uric acid hydroxylation. This suggests that Arg204 facilitates the deprotonation of uric acid activating it for the oxygen transfer. Based on these data, a mechanism for this reaction is proposed consisting of a nucleophilic attack of the urate anion on the flavin hydroperoxide resulting in the formation of 5-hydroxyisourate. Structural and Mechanistic Studies of HpxO, a Novel FAD-dependent Urate Oxidase from Klebsiella pneumoniae.,Hicks KA, O'Leary SE, Begley TP, Ealick SE Biochemistry. 2012 Dec 21. PMID:23259842 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Monooxygenase 3D structures

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