2ivf
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Anaerobic degradation of hydrocarbons was discovered a decade ago, and | + | 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== | ==About this Structure== | ||
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[[Category: Hagel, C.]] | [[Category: Hagel, C.]] | ||
[[Category: Heider, J.]] | [[Category: Heider, J.]] | ||
| - | [[Category: Kloer, D | + | [[Category: Kloer, D P.]] |
| - | [[Category: Schulz, G | + | [[Category: Schulz, G E.]] |
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: F3S]] | [[Category: F3S]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:56:26 2008'' |
Revision as of 15:56, 21 February 2008
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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 , , , , , , , , and as ligands. Active as Ethylbenzene hydroxylase, with EC number 1.17.99.2 Known structural/functional Site: . 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 Thu Feb 21 17:56:26 2008
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
