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| | <StructureSection load='1uli' size='340' side='right'caption='[[1uli]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='1uli' size='340' side='right'caption='[[1uli]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1uli]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhojr Rhojr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ULI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1uli]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_jostii_RHA1 Rhodococcus jostii RHA1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ULI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ULI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ulj|1ulj]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Biphenyl_2,3-dioxygenase Biphenyl 2,3-dioxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.12.18 1.14.12.18] </span></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=1uli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uli OCA], [https://pdbe.org/1uli PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uli RCSB], [https://www.ebi.ac.uk/pdbsum/1uli PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uli ProSAT]</span></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=1uli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uli OCA], [https://pdbe.org/1uli PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uli RCSB], [https://www.ebi.ac.uk/pdbsum/1uli PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uli ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/BPHA1_RHOJR BPHA1_RHOJR] Part of the oxygenase component of the biphenyl dioxygenase system that catalyzes the stereospecific dihydroxylation of the aromatic ring of biphenyl, yielding a dihydrodiol compound. Is essential for biphenyl degradation and growth of Rhodococcus sp. strain RHA1 on biphenyl as the sole source of carbon and energy. Can also use naphtalene and 4-chlorobiphenyl (4-CB) as substrates, as well as some polychlorinated biphenyls (PCB) such as 2,2'-dichlorobiphenyl, 2,3-dichlorobiphenyl and 2,5,2'-trichlorobiphenyl. Exhibits weak activity toward dibenzofuran and dibenzo-p-dioxin. Electrons are transferred from NADH to the [2Fe-2S] cluster in BphA1 via FAD of BphA4 and [2Fe-2S] cluster of BphA3.<ref>PMID:17420585</ref> <ref>PMID:7793929</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Biphenyl 2,3-dioxygenase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Rhojr]] | + | [[Category: Rhodococcus jostii RHA1]] |
| - | [[Category: Fukuda, M]] | + | [[Category: Fukuda M]] |
| - | [[Category: Furusawa, Y]] | + | [[Category: Furusawa Y]] |
| - | [[Category: Masai, E]] | + | [[Category: Masai E]] |
| - | [[Category: Nagarajan, V]] | + | [[Category: Nagarajan V]] |
| - | [[Category: Senda, T]] | + | [[Category: Senda T]] |
| - | [[Category: Tanokura, M]] | + | [[Category: Tanokura M]] |
| - | [[Category: Alpha3 beta3 hetero hexamer]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
BPHA1_RHOJR Part of the oxygenase component of the biphenyl dioxygenase system that catalyzes the stereospecific dihydroxylation of the aromatic ring of biphenyl, yielding a dihydrodiol compound. Is essential for biphenyl degradation and growth of Rhodococcus sp. strain RHA1 on biphenyl as the sole source of carbon and energy. Can also use naphtalene and 4-chlorobiphenyl (4-CB) as substrates, as well as some polychlorinated biphenyls (PCB) such as 2,2'-dichlorobiphenyl, 2,3-dichlorobiphenyl and 2,5,2'-trichlorobiphenyl. Exhibits weak activity toward dibenzofuran and dibenzo-p-dioxin. Electrons are transferred from NADH to the [2Fe-2S] cluster in BphA1 via FAD of BphA4 and [2Fe-2S] cluster of BphA3.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Biphenyl dioxygenase is the enzyme that catalyzes the stereospecific dioxygenation of the aromatic ring. This enzyme has attracted the attention of researchers due to its ability to oxidize polychlorinated biphenyls, which is one of the serious environmental contaminants. We determined the crystal structure of the terminal oxygenase component of the biphenyl dioxygenase (BphA1A2) derived from Rhodococcus strain sp. RHA1 in substrate-free and complex forms. These crystal structures revealed that the substrate-binding pocket makes significant conformational changes upon substrate binding to accommodate the substrate into the pocket. Our analysis of the crystal structures suggested that the residues in the substrate-binding pocket can be classified into three groups, which, respectively, seem to be responsible for the catalytic reaction, the orientation/conformation of the substrate, and the conformational changes of the substrate-binding pocket. The cooperative actions of residues in the three groups seem to determine the substrate specificity of the enzyme.
Crystal structure of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1.,Furusawa Y, Nagarajan V, Tanokura M, Masai E, Fukuda M, Senda T J Mol Biol. 2004 Sep 17;342(3):1041-52. PMID:15342255[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Iwasaki T, Takeda H, Miyauchi K, Yamada T, Masai E, Fukuda M. Characterization of two biphenyl dioxygenases for biphenyl/PCB degradation in A PCB degrader, Rhodococcus sp. strain RHA1. Biosci Biotechnol Biochem. 2007 Apr;71(4):993-1002. PMID:17420585 doi:10.1271/bbb.60663
- ↑ Masai E, Yamada A, Healy JM, Hatta T, Kimbara K, Fukuda M, Yano K. Characterization of biphenyl catabolic genes of gram-positive polychlorinated biphenyl degrader Rhodococcus sp. strain RHA1. Appl Environ Microbiol. 1995 Jun;61(6):2079-85. PMID:7793929 doi:10.1128/aem.61.6.2079-2085.1995
- ↑ Furusawa Y, Nagarajan V, Tanokura M, Masai E, Fukuda M, Senda T. Crystal structure of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1. J Mol Biol. 2004 Sep 17;342(3):1041-52. PMID:15342255 doi:10.1016/j.jmb.2004.07.062
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