View source for 5brt


==Crystal Structure of 2-hydroxybiphenyl 3-monooxygenase from Pseudomonas azelaica with 2-hydroxybiphenyl in the active site==
<StructureSection load='5brt' size='340' side='right'caption='[[5brt]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5brt]] is a 2 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=5BRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BRT 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CH9:2-HYDROXYBIPHENYL'>CH9</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=5brt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5brt OCA], [https://pdbe.org/5brt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5brt RCSB], [https://www.ebi.ac.uk/pdbsum/5brt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5brt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O06647_9PSED O06647_9PSED] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
2-Hydroxybiphenyl 3-monooxygenase (HbpA) is an FAD dependent monooxygenase which catalyzes the ortho-hydroxylation of a broad range of 2-substituted phenols in the presence of NADH and molecular oxygen. We have determined the structure of HbpA from the soil bacterium Pseudomonas azelaica HBP1 with bound 2-hydroxybiphenyl, as well as several variants, at a resolution of 2.3-2.5A to investigate structure function correlations of the enzyme. An observed hydrogen bond between 2-hydroxybiphenyl and His48 in the active site confirmed the previously suggested role of this residue in substrate deprotonation. The entrance to the active site was confirmed by generating variant G255F which exhibited only about 7% of the wild-type's specific activity of product formation, suggesting inhibition of substrate entrance into the active site by the large aromatic residue. Residue Arg242 is suggested to facilitate FAD movement and reduction as was previously reported in studies on the homologous protein para-hydroxybenzoate hydroxylase. In addition, it is suggested that Trp225, which is located in the active site, facilitates proper substrate entrance into the binding pocket in contrast to aklavinone-11-hydroxylase and para-hydroxybenzoate hydroxylase in which a residue at a similar position is responsible for substrate deprotonation. Structure function correlations described in this work will aid in the design of variants with improved activity and altered selectivity for potential industrial applications.

A crystal structure of 2-hydroxybiphenyl 3-monooxygenase with bound substrate provides insights into the enzymatic mechanism.,Kanteev M, Bregman-Cohen A, Deri B, Shahar A, Adir N, Fishman A Biochim Biophys Acta. 2015 Aug 11. pii: S1570-9639(15)00206-X. doi:, 10.1016/j.bbapap.2015.08.002. PMID:26275805<ref>PMID:26275805</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5brt" style="background-color:#fffaf0;"></div>

==See Also==
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas nitroreducens HBP1]]
[[Category: Adir N]]
[[Category: Bregman-Cohen A]]
[[Category: Deri B]]
[[Category: Fishman A]]
[[Category: Kanteev M]]