2ivf
From Proteopedia
|
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 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
Page seeded by OCA on Mon Nov 5 18:17:46 2007
Categories: Azoarcus sp. eb1 | Ethylbenzene hydroxylase | Protein complex | Hagel, C. | Heider, J. | Kloer, D.P. | Schulz, G.E. | ACT | F3S | GOL | HEM | MD1 | MES | MGD | MO | PO4 | SF4 | Anaerobic hydrocarbon degradation | Dmso reductase family | Fe/s cluster | Mo-bismgd enzyme | Moco | Oxidoreductase
