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1ddo

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(New page: 200px<br /> <applet load="1ddo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ddo, resolution 3.1&Aring;" /> '''REDUCED D-AMINO ACID...)
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Revision as of 18:19, 29 October 2007

Image:1ddo.gif

1ddo, resolution 3.1Å

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REDUCED D-AMINO ACID OXIDASE FROM PIG KIDNEY IN COMPLEX WITH IMINO-TRP

Overview

D-Amino acid oxidase (DAAO) is the prototype of the flavin-containing, oxidases. It catalyzes the oxidative deamination of various D-amino acids, ranging from D-Ala to D-Trp. We have carried out the X-ray analysis of, reduced DAAO in complex with the reaction product imino tryptophan (iTrp), and of the covalent adduct generated by the photoinduced reaction of the, flavin with 3-methyl-2-oxobutyric acid (kVal). These structures were, solved by combination of 8-fold density averaging and least-squares, refinement techniques. The FAD redox state of DAAO crystals was assessed, by single-crystal polarized absorption microspectrophotometry. iTrp binds, to the reduced enzyme with the N, C alpha, C, and C beta atoms positioned, 3.8 A from the re side of the flavin. The indole side chain points ... [(full description)]

About this Structure

1DDO is a [Single protein] structure of sequence from [Sus scrofa] with FAD, ITR and DTR as [ligands]. Active as [[1]], with EC number [1.4.3.3]. Full crystallographic information is available from [OCA].

Reference

Active site plasticity in D-amino acid oxidase: a crystallographic analysis., Todone F, Vanoni MA, Mozzarelli A, Bolognesi M, Coda A, Curti B, Mattevi A, Biochemistry. 1997 May 13;36(19):5853-60. PMID:9153426

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