2c12

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Image:2c12.gif

2c12, resolution 2.07Å

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CRYSTAL STRUCTURE OF NITROALKANE OXIDASE IN COMPLEX WITH SPERMINE, A COMPETITIVE INHIBITOR

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

2C12 is a [Single protein] structure of sequence from [Fusarium oxysporum] with SPM, FAD, PE4 and GOL as [ligands]. Structure known Active Site: AC1. 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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