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| | <StructureSection load='4cy6' size='340' side='right'caption='[[4cy6]], [[Resolution|resolution]] 2.76Å' scene=''> | | <StructureSection load='4cy6' size='340' side='right'caption='[[4cy6]], [[Resolution|resolution]] 2.76Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4cy6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_azelaica_hbp1 Pseudomonas azelaica hbp1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CY6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4cy6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_nitroreducens_HBP1 Pseudomonas nitroreducens HBP1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CY6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CY6 FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-hydroxybiphenyl_3-monooxygenase 2-hydroxybiphenyl 3-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.44 1.14.13.44] </span></td></tr> | + | </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=4cy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cy6 OCA], [https://pdbe.org/4cy6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cy6 RCSB], [https://www.ebi.ac.uk/pdbsum/4cy6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cy6 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cy6 OCA], [http://pdbe.org/4cy6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cy6 RCSB], [http://www.ebi.ac.uk/pdbsum/4cy6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cy6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [[https://www.uniprot.org/uniprot/O06647_9PSED O06647_9PSED]] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Monooxygenase|Monooxygenase]] | + | *[[Monooxygenase 3D structures|Monooxygenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 2-hydroxybiphenyl 3-monooxygenase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseudomonas azelaica hbp1]] | + | [[Category: Pseudomonas nitroreducens HBP1]] |
| - | [[Category: Farrugia, J E]] | + | [[Category: Farrugia JE]] |
| - | [[Category: Frank, A]] | + | [[Category: Frank A]] |
| - | [[Category: Grogan, G]] | + | [[Category: Grogan G]] |
| - | [[Category: Hart, S]] | + | [[Category: Hart S]] |
| - | [[Category: Jensen, C N]] | + | [[Category: Jensen CN]] |
| - | [[Category: Man, H]] | + | [[Category: Man H]] |
| - | [[Category: Turkenburg, J P]] | + | [[Category: Turkenburg JP]] |
| - | [[Category: Fad]]
| + | |
| - | [[Category: Flavin]]
| + | |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Hydroxylation]]
| + | |
| - | [[Category: Nadh]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
[O06647_9PSED]
Publication Abstract from PubMed
The FAD-dependent monooxygenase HbpA from Pseudomonas azelaica HBP1 catalyses the hydroxylation of 2-hydroxybiphenyl (2HBP) to 2,3-dihydroxybiphenyl (23DHBP). HbpA has been used extensively as a model for studying flavoprotein hydroxylases under process conditions, and has also been subjected to directed-evolution experiments that altered its catalytic properties. The structure of HbpA has been determined in its apo and FAD-complex forms to resolutions of 2.76 and 2.03 A, respectively. Comparisons of the HbpA structure with those of homologues, in conjunction with a model of the reaction product in the active site, reveal His48 as the most likely acid/base residue to be involved in the hydroxylation mechanism. Mutation of His48 to Ala resulted in an inactive enzyme. The structures of HbpA also provide evidence that mutants achieved by directed evolution that altered activity are comparatively remote from the substrate-binding site.
Structures of the Apo and FAD-Bound Forms of 2-Hydroxybiphenyl 3-monooxygenase (HbpA) Locate Activity Hotspots Identified by Using Directed Evolution.,Jensen CN, Mielke T, Farrugia JE, Frank A, Man H, Hart S, Turkenburg JP, Grogan G Chembiochem. 2015 Mar 3. doi: 10.1002/cbic.201402701. PMID:25737306[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jensen CN, Mielke T, Farrugia JE, Frank A, Man H, Hart S, Turkenburg JP, Grogan G. Structures of the Apo and FAD-Bound Forms of 2-Hydroxybiphenyl 3-monooxygenase (HbpA) Locate Activity Hotspots Identified by Using Directed Evolution. Chembiochem. 2015 Mar 3. doi: 10.1002/cbic.201402701. PMID:25737306 doi:http://dx.doi.org/10.1002/cbic.201402701
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