3n2s: Difference between revisions

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<StructureSection load='3n2s' size='340' side='right' caption='[[3n2s]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='3n2s' size='340' side='right' caption='[[3n2s]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3n2s]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3N2S FirstGlance]. <br>
<table><tr><td colspan='2'>[[3n2s]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3N2S FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nfrA1, nfrA, ywcG, BSU38110, ipa-43d ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nfrA1, nfrA, ywcG, BSU38110, ipa-43d ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.38, 1.5.1.39 and 1.5.1.41 1.5.1.38, 1.5.1.39 and 1.5.1.41] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.38, 1.5.1.39 and 1.5.1.41 1.5.1.38, 1.5.1.39 and 1.5.1.41] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3n2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n2s OCA], [http://pdbe.org/3n2s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3n2s RCSB], [http://www.ebi.ac.uk/pdbsum/3n2s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3n2s ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3n2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n2s OCA], [http://pdbe.org/3n2s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3n2s RCSB], [http://www.ebi.ac.uk/pdbsum/3n2s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3n2s ProSAT]</span></td></tr>
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n2/3n2s_consurf.spt"</scriptWhenChecked>
     <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/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus globigii migula 1900]]
[[Category: Vibrio subtilis ehrenberg 1835]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Cortial, S]]
[[Category: Cortial, S]]

Revision as of 16:24, 16 January 2019

Structure of NfrA1 nitroreductase from B. subtilisStructure of NfrA1 nitroreductase from B. subtilis

Structural highlights

3n2s is a 4 chain structure with sequence from "vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
NonStd Res:
Gene:nfrA1, nfrA, ywcG, BSU38110, ipa-43d ("Vibrio subtilis" Ehrenberg 1835)
Activity:Oxidoreductase, with EC number 1.5.1.39 and 1.5.1.41 1.5.1.38, 1.5.1.39 and 1.5.1.41
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NFRA1_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 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[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Zenno S, Kobori T, Tanokura M, Saigo K. Purification and characterization of NfrA1, a Bacillus subtilis nitro/flavin reductase capable of interacting with the bacterial luciferase. Biosci Biotechnol Biochem. 1998 Oct;62(10):1978-87. PMID:9836433 doi:http://dx.doi.org/10.1271/bbb.62.1978
  2. ↑ Cortial S, Chaignon P, Iorga BI, Aymerich S, Truan G, Gueguen-Chaignon V, Meyer P, Morera S, Ouazzani J. NADH oxidase activity of Bacillus subtilis nitroreductase NfrA1: Insight into its biological role. FEBS Lett. 2010 Aug 18. PMID:20727352 doi:10.1016/j.febslet.2010.08.019

3n2s, resolution 1.95Å

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