4cy6: Difference between revisions
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==apo structure of 2-hydroxybiphenyl 3-monooxygenase HbpA== | ==apo structure of 2-hydroxybiphenyl 3-monooxygenase HbpA== | ||
<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. 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 [ | <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=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.76Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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> | ||
</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 == | ||
| Line 14: | Line 17: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4cy6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Farrugia | [[Category: Pseudomonas nitroreducens HBP1]] | ||
[[Category: Frank | [[Category: Farrugia JE]] | ||
[[Category: Grogan | [[Category: Frank A]] | ||
[[Category: Hart | [[Category: Grogan G]] | ||
[[Category: Jensen | [[Category: Hart S]] | ||
[[Category: Man | [[Category: Jensen CN]] | ||
[[Category: Turkenburg | [[Category: Man H]] | ||
[[Category: Turkenburg JP]] | |||
Latest revision as of 15:17, 20 December 2023
apo structure of 2-hydroxybiphenyl 3-monooxygenase HbpAapo structure of 2-hydroxybiphenyl 3-monooxygenase HbpA
Structural highlights
FunctionPublication Abstract from PubMedThe 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 AlsoReferences
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