4z2r: Difference between revisions
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The | ==Crystal structure of 2-hydroxybiphenyl 3-monooxygenase from Pseudomonas azelaica== | ||
<StructureSection load='4z2r' size='340' side='right'caption='[[4z2r]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4z2r]] 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=4Z2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z2R 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]] 2.3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=4z2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z2r OCA], [https://pdbe.org/4z2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z2r RCSB], [https://www.ebi.ac.uk/pdbsum/4z2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z2r 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 4z2r" style="background-color:#fffaf0;"></div> | ||
[[Category: Bregman-Cohen | |||
[[Category: Fishman | ==See Also== | ||
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas nitroreducens HBP1]] | |||
[[Category: Bregman-Cohen A]] | |||
[[Category: Fishman A]] | |||
[[Category: Kanteev M]] | |||
Latest revision as of 14:32, 9 May 2024
Crystal structure of 2-hydroxybiphenyl 3-monooxygenase from Pseudomonas azelaicaCrystal structure of 2-hydroxybiphenyl 3-monooxygenase from Pseudomonas azelaica
Structural highlights
FunctionPublication Abstract from PubMed2-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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