2cdu
From Proteopedia
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THE CRYSTAL STRUCTURE OF WATER-FORMING NAD(P)H OXIDASE FROM LACTOBACILLUS SANFRANCISCENSIS
Overview
The FAD-dependent NAD(P)H oxidase from Lactobacillus sanfrancisensis, (L.san-Nox2) catalyzes the oxidation of 2 equivalents of either NADH or, NADPH and reduces 1 equivalent of O(2) to yield 2 equivalents of water., During steady-state turnover only 0.5% of the reducing equivalents are, detected in solution as hydrogen peroxide, suggesting that it is not, released from the enzyme after the oxidation of the first equivalent of, NAD(P)H and reaction with O(2). Here we report the crystal structure of, L.san-Nox2 to 1.8 A resolution. The enzyme crystallizes as a dimer with, each monomer consisting of a FAD binding domain (residues 1-120), a, NAD(P)H binding domain (residues 150-250), and a dimerization domain, (residues 325-451). The electron density for the redox-active Cys42, residue ... [(full description)]
About this Structure
2CDU is a [Single protein] structure of sequence from [Lactobacillus sanfranciscensis] with FAD and ADP as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
The crystal structure of NAD(P)H oxidase from Lactobacillus sanfranciscensis: insights into the conversion of O2 into two water molecules by the flavoenzyme., Lountos GT, Jiang R, Wellborn WB, Thaler TL, Bommarius AS, Orville AM, Biochemistry. 2006 Aug 15;45(32):9648-59. PMID:16893166
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