3n2s: Difference between revisions
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New page: '''Unreleased structure''' The entry 3n2s is ON HOLD Authors: Morera, S., Gueguen-Chaignon, V., Meyer, P., Cortial, S., Ouazzani, J. Description: Structure of NfrA1 nitroreductase from... |
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==Structure of NfrA1 nitroreductase from B. subtilis== | |||
<StructureSection load='3n2s' size='340' side='right'caption='[[3n2s]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3n2s]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N2S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N2S 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]] 1.95Å</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=MSE:SELENOMETHIONINE'>MSE</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=3n2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n2s OCA], [https://pdbe.org/3n2s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n2s RCSB], [https://www.ebi.ac.uk/pdbsum/3n2s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n2s ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/NFRA1_BACSU NFRA1_BACSU] Reduces FMNH(2) to FMN, with NADPH as reductant. It also reduces nitroaromatic compounds, quinones and azo dyes.<ref>PMID:9836433</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n2/3n2s_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3n2s ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
NfrA1 nitroreductase from the Gram-positive bacterium Bacillus subtilis is a member of the NAD(P)H/FMN oxidoreductase family. Here, we investigated the reactivity, the structure and kinetics of NfrA1, which could provide insight into the unclear biological role of this enzyme. We could show that NfrA1 possesses an NADH oxidase activity that leads to high concentrations of oxygen peroxide and an NAD(+) degrading activity leading to free nicotinamide. Finally, we showed that NfrA1 is able to rapidly scavenge H(2)O(2) produced during the oxidative process or added exogenously. STRUCTURED SUMMARY: MINT-7990140: nfrA1 (uniprotkb:P39605) and nfrA1 (uniprotkb:P39605) bind (MI:0407) by X-ray crystallography (MI:0114). | |||
NADH oxidase activity of Bacillus subtilis nitroreductase NfrA1: Insight into its biological role.,Cortial S, Chaignon P, Iorga BI, Aymerich S, Truan G, Gueguen-Chaignon V, Meyer P, Morera S, Ouazzani J FEBS Lett. 2010 Aug 18. PMID:20727352<ref>PMID:20727352</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3n2s" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Nitroreductase 3D structures|Nitroreductase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus subtilis]] | |||
[[Category: Large Structures]] | |||
[[Category: Cortial S]] | |||
[[Category: Gueguen-Chaignon V]] | |||
[[Category: Meyer P]] | |||
[[Category: Morera S]] | |||
[[Category: Ouazzani J]] | |||
Latest revision as of 13:12, 6 November 2024
Structure of NfrA1 nitroreductase from B. subtilisStructure of NfrA1 nitroreductase from B. subtilis
Structural highlights
FunctionNFRA1_BACSU Reduces FMNH(2) to FMN, with NADPH as reductant. It also reduces nitroaromatic compounds, quinones and azo dyes.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedNfrA1 nitroreductase from the Gram-positive bacterium Bacillus subtilis is a member of the NAD(P)H/FMN oxidoreductase family. Here, we investigated the reactivity, the structure and kinetics of NfrA1, which could provide insight into the unclear biological role of this enzyme. We could show that NfrA1 possesses an NADH oxidase activity that leads to high concentrations of oxygen peroxide and an NAD(+) degrading activity leading to free nicotinamide. Finally, we showed that NfrA1 is able to rapidly scavenge H(2)O(2) produced during the oxidative process or added exogenously. STRUCTURED SUMMARY: MINT-7990140: nfrA1 (uniprotkb:P39605) and nfrA1 (uniprotkb:P39605) bind (MI:0407) by X-ray crystallography (MI:0114). NADH oxidase activity of Bacillus subtilis nitroreductase NfrA1: Insight into its biological role.,Cortial S, Chaignon P, Iorga BI, Aymerich S, Truan G, Gueguen-Chaignon V, Meyer P, Morera S, Ouazzani J FEBS Lett. 2010 Aug 18. PMID:20727352[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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