2c0u | pdb_00002c0u
CRYSTAL STRUCTURE OF A COVALENT COMPLEX OF NITROALKANE OXIDASE TRAPPED DURING SUBSTRATE TURNOVER
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Overview
Nitroalkane oxidase (NAO) from Fusarium oxysporum catalyzes the oxidation, of neutral nitroalkanes to the corresponding aldehydes or ketones with the, production of H(2)O(2) and nitrite. The flavoenzyme is a new member of the, acyl-CoA dehydrogenase (ACAD) family, but it does not react with acyl-CoA, substrates. We present the 2.2 A resolution crystal structure of NAO, trapped during the turnover of nitroethane as a covalent N5-FAD adduct, (ES*). The homotetrameric structure of ES* was solved by MAD phasing with, 52 Se-Met sites in an orthorhombic space group. The electron density for, the N5-(2-nitrobutyl)-1,5-dihydro-FAD covalent intermediate is clearly, resolved. The structure of ES was used to solve the crystal structure of, oxidized NAO at 2.07 A resolution. The c axis for the ... [(full description)]
About this Structure
2C0U is a [Single protein] structure of sequence from [Fusarium oxysporum] with FAD as [ligand]. Full crystallographic information is available from [OCA].
Reference
Crystal structures of nitroalkane oxidase: insights into the reaction mechanism from a covalent complex of the flavoenzyme trapped during turnover., Nagpal A, Valley MP, Fitzpatrick PF, Orville AM, Biochemistry. 2006 Jan 31;45(4):1138-50. PMID:16430210
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