2ivf

From Proteopedia

Revision as of 15:12, 30 October 2007

ETHYLBENZENE DEHYDROGENASE FROM AROMATOLEUM AROMATICUM

Overview

Anaerobic degradation of hydrocarbons was discovered a decade ago, and, ethylbenzene dehydrogenase was one of the first characterized enzymes, involved. The structure of the soluble periplasmic 165 kDa enzyme was, established at 1.88 A resolution. It is a heterotrimer. The alpha subunit, contains the catalytic center with a molybdenum held by two, molybdopterin-guanine dinucleotides, one with an open pyran ring, and an, iron-sulfur cluster with a histidine ligand. During catalysis, electrons, produced by substrate oxidation are transferred to a heme in the gamma, subunit and then presumably to a separate cytochrome involved in nitrate, respiration. The beta subunit contains four iron-sulfur clusters and is, structurally related to ferredoxins. The gamma subunit is the first known, protein ... [(full description)]

About this Structure

2IVF is a [Protein complex] structure of sequences from [Azoarcus sp. eb1] with ACT, PO4, MES, SF4, MO, MGD, MD1, F3S, HEM and GOL as [ligands]. Active as [Ethylbenzene hydroxylase], with EC number [1.17.99.2]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Crystal structure of ethylbenzene dehydrogenase from Aromatoleum aromaticum., Kloer DP, Hagel C, Heider J, Schulz GE, Structure. 2006 Sep;14(9):1377-88. PMID:16962969

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