8qyg
From Proteopedia
(Difference between revisions)
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<table><tr><td colspan='2'>[[8qyg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_tequilensis Bacillus tequilensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8QYG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QYG FirstGlance]. <br> | <table><tr><td colspan='2'>[[8qyg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_tequilensis Bacillus tequilensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8QYG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QYG 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]] 1.15Å</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]] 1.15Å</td></tr> | ||
| - | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=8qyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qyg OCA], [https://pdbe.org/8qyg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qyg RCSB], [https://www.ebi.ac.uk/pdbsum/8qyg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qyg 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=8qyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qyg OCA], [https://pdbe.org/8qyg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qyg RCSB], [https://www.ebi.ac.uk/pdbsum/8qyg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qyg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/A0A6H0WK49_9BACI A0A6H0WK49_9BACI] | [https://www.uniprot.org/uniprot/A0A6H0WK49_9BACI A0A6H0WK49_9BACI] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Nitroreductases (NRs) are NAD(P)H-dependent flavoenzymes that reduce nitro aromatic compounds to their corresponding arylamines via the nitroso and hydroxylamine intermediates. Because of their broad substrate scope and versatility, NRs have found application in multiple fields such as biocatalysis, bioremediation, cell-imaging and prodrug activation. However, only a limited number of members of the broad NR superfamily (> 24 000 sequences) have been experimentally characterized. Within this group of enzymes, only few are capable of amine synthesis, which is a fundamental chemical transformation for the pharmaceutical, agricultural, and textile industries. Herein, we provide a comprehensive description of a recently discovered NR from Bacillus tequilensis, named BtNR. This enzyme has previously been demonstrated to have the capability to fully convert nitro aromatic and heterocyclic compounds to their respective primary amines. In this study, we determined its biochemical, kinetic and structural properties, including its apparent melting temperature (T(m)) of 59 degrees C, broad pH activity range (from pH 3 to 10) and a notably low redox potential (-236 +/- 1 mV) in comparison to other well-known NRs. We also determined its steady-state and pre-steady-state kinetic parameters, which are consistent with other NRs. Additionally, we elucidated the crystal structure of BtNR, which resembles the well-characterized Escherichia coli oxygen-insensitive NAD(P)H nitroreductase (NfsB), and investigated the substrate binding in its active site through docking and molecular dynamics studies with four nitro aromatic substrates. Guided by these structural analyses, we probed the functional roles of active site residues by site-directed mutagenesis. Our findings provide valuable insights into the biochemical and structural properties of BtNR, as well as its potential applications in biotechnology. | ||
| + | |||
| + | Biochemical, kinetic, and structural characterization of a Bacillus tequilensis nitroreductase.,Russo S, Rozeboom HJ, Wijma HJ, Poelarends GJ, Fraaije MW FEBS J. 2024 Jul 1. doi: 10.1111/febs.17210. PMID:38946302<ref>PMID:38946302</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8qyg" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of Nitroreductase from Bacillus tequilensis
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