2ivf
From Proteopedia
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| - | [[Image:2ivf.jpg|left|200px]]<br /><applet load="2ivf" size=" | + | [[Image:2ivf.jpg|left|200px]]<br /><applet load="2ivf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ivf, resolution 1.88Å" /> | caption="2ivf, resolution 1.88Å" /> | ||
'''ETHYLBENZENE DEHYDROGENASE FROM AROMATOLEUM AROMATICUM'''<br /> | '''ETHYLBENZENE DEHYDROGENASE FROM AROMATOLEUM AROMATICUM'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2IVF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Azoarcus_sp._eb1 Azoarcus sp. eb1] with ACT, PO4, MES, SF4, MO, MGD, MD1, F3S, HEM and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ethylbenzene_hydroxylase Ethylbenzene hydroxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.99.2 1.17.99.2] Known structural/functional Site: <scene name='pdbsite=AC1:Md1 Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2IVF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Azoarcus_sp._eb1 Azoarcus sp. eb1] with <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=MES:'>MES</scene>, <scene name='pdbligand=SF4:'>SF4</scene>, <scene name='pdbligand=MO:'>MO</scene>, <scene name='pdbligand=MGD:'>MGD</scene>, <scene name='pdbligand=MD1:'>MD1</scene>, <scene name='pdbligand=F3S:'>F3S</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ethylbenzene_hydroxylase Ethylbenzene hydroxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.99.2 1.17.99.2] Known structural/functional Site: <scene name='pdbsite=AC1:Md1+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IVF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:38:38 2008'' |
Revision as of 08:38, 3 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
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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
