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New page: left|200px<br /> <applet load="2ivf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ivf, resolution 1.88Å" /> '''ETHYLBENZENE DEHYDR...
 
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[[Image:2ivf.gif|left|200px]]<br />
<applet load="2ivf" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2ivf, resolution 1.88&Aring;" />
'''ETHYLBENZENE DEHYDROGENASE FROM AROMATOLEUM AROMATICUM'''<br />


==Overview==
==Ethylbenzene dehydrogenase from Aromatoleum aromaticum==
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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?16962969 (full description)]]
<StructureSection load='2ivf' size='340' side='right'caption='[[2ivf]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ivf]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Aromatoleum_aromaticum_EbN1 Aromatoleum aromaticum EbN1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IVF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IVF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.88&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MD1:PHOSPHORIC+ACID+4-(2-AMINO-4-OXO-3,4,5,6,-TETRAHYDRO-PTERIDIN-6-YL)-2-HYDROXY-3,4-DIMERCAPTO-BUT-3-EN-YL+ESTER+GUANYLATE+ESTER'>MD1</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MGD:2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE+GUANOSINE+DINUCLEOTIDE'>MGD</scene>, <scene name='pdbligand=MO:MOLYBDENUM+ATOM'>MO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ivf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ivf OCA], [https://pdbe.org/2ivf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ivf RCSB], [https://www.ebi.ac.uk/pdbsum/2ivf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ivf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5P5I0_AROAE Q5P5I0_AROAE]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iv/2ivf_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ivf ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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==
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<ref>PMID:16962969</ref>
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/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.17.99.2 1.17.99.2]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IVF OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of ethylbenzene dehydrogenase from Aromatoleum aromaticum., Kloer DP, Hagel C, Heider J, Schulz GE, Structure. 2006 Sep;14(9):1377-88. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16962969 16962969]
</div>
[[Category: Azoarcus sp. eb1]]
<div class="pdbe-citations 2ivf" style="background-color:#fffaf0;"></div>
[[Category: Protein complex]]
== References ==
[[Category: Hagel, C.]]
<references/>
[[Category: Heider, J.]]
__TOC__
[[Category: Kloer, D.P.]]
</StructureSection>
[[Category: Schulz, G.E.]]
[[Category: Aromatoleum aromaticum EbN1]]
[[Category: ACT]]
[[Category: Large Structures]]
[[Category: F3S]]
[[Category: Hagel C]]
[[Category: GOL]]
[[Category: Heider J]]
[[Category: HEM]]
[[Category: Kloer DP]]
[[Category: MD1]]
[[Category: Schulz GE]]
[[Category: MES]]
[[Category: MGD]]
[[Category: MO]]
[[Category: PO4]]
[[Category: SF4]]
[[Category: anaerobic hydrocarbon degradation]]
[[Category: dmso reductase family]]
[[Category: fe/s cluster]]
[[Category: mo-bismgd enzyme]]
[[Category: moco]]
[[Category: oxidoreductase]]
 
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Latest revision as of 17:22, 8 September 2026

Ethylbenzene dehydrogenase from Aromatoleum aromaticum

2ivf, resolution 1.88Å

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