2ivf

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Image:2ivf.jpg

, resolution 1.88Å

Sites:

Ligands:

, , , , , , , , and

Activity:

Ethylbenzene hydroxylase, with EC number 1.17.99.2

Coordinates:

save as pdb, mmCIF, xml

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 with a methionine and a lysine as axial heme ligands. The catalytic product was modeled into the active center, showing the reaction geometry. A mechanism consistent with activity and inhibition data of ethylbenzene-related compounds is proposed.

About this Structure

2IVF is a Protein complex structure of sequences from Azoarcus sp. eb1. 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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