2gjl

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(New page: 200px<br /><applet load="2gjl" size="350" color="white" frame="true" align="right" spinBox="true" caption="2gjl, resolution 2.000&Aring;" /> '''Crystal Structure o...)
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[[Image:2gjl.gif|left|200px]]<br /><applet load="2gjl" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2gjl, resolution 2.000&Aring;" />
 
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'''Crystal Structure of 2-nitropropane dioxygenase'''<br />
 
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==Overview==
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==Crystal Structure of 2-nitropropane dioxygenase==
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Nitroalkane compounds are widely used in chemical industry and are also, produced by microorganisms and plants. Some nitroalkanes have been, demonstrated to be carcinogenic, and enzymatic oxidation of nitroalkanes, is of considerable interest. 2-Nitropropane dioxygenases from Neurospora, crassa and Williopsis mrakii (Hansenula mrakii), members of one family of, the nitroalkane-oxidizing enzymes, contain FMN and FAD, respectively. The, enzymatic oxidation of nitroalkanes by 2-nitropropane dioxygenase operates, by an oxidase-style catalytic mechanism, which was recently shown to, involve the formation of an anionic flavin semiquinone. This represents a, unique case in which an anionic flavin semiquinone has been experimentally, observed in the catalytic pathway for oxidation catalyzed by a, flavin-dependent enzyme. Here we report the first crystal structure of, 2-nitropropane dioxygenase from Pseudomonas aeruginosa in two forms: a, binary complex with FMN and a ternary complex with both FMN and, 2-nitropropane. The structure identifies His(152) as the proposed, catalytic base, thus providing a structural framework for a better, understanding of the catalytic mechanism.
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<StructureSection load='2gjl' size='340' side='right'caption='[[2gjl]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[2gjl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GJL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GJL FirstGlance]. <br>
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2GJL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=FMN:'>FMN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/2-nitropropane_dioxygenase 2-nitropropane dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.32 1.13.11.32] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GJL OCA].
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</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&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gjl OCA], [https://pdbe.org/2gjl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gjl RCSB], [https://www.ebi.ac.uk/pdbsum/2gjl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gjl ProSAT]</span></td></tr>
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Crystal structure of 2-nitropropane dioxygenase complexed with FMN and substrate. Identification of the catalytic base., Ha JY, Min JY, Lee SK, Kim HS, Kim do J, Kim KH, Lee HH, Kim HK, Yoon HJ, Suh SW, J Biol Chem. 2006 Jul 7;281(27):18660-7. Epub 2006 May 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16682407 16682407]
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</table>
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[[Category: 2-nitropropane dioxygenase]]
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== Function ==
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[[Category: Pseudomonas aeruginosa]]
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[https://www.uniprot.org/uniprot/NQRED_PSEAE NQRED_PSEAE] Catalyzes the NADH-dependent reduction of a broad spectrum of quinone substrates, generating the corresponding hydroquinones. Highly prefers NADH to NADPH as a reducing substrate. Also displays a small NADH oxidase activity. Does not exhibit nitronate monooxygenase activity; is inactive against propionate 3-nitronate, 3-nitropropionate, nitroethane, 1-nitropropane, 2-nitropropane, and the anionic forms ethylnitronate, propyl-1-nitronate, and propyl-2-nitronate. Has no azoreductase activity since it is not able to reduce the azo dye methyl red with NADH. May be required to maintain an appropriate [NAD(+)]/[NADH] ratio for the catabolism of fatty acids in P.aeruginosa PAO1.<ref>PMID:27502282</ref>
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[[Category: Single protein]]
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== Evolutionary Conservation ==
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[[Category: Suh, S.W.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: FMN]]
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Check<jmol>
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[[Category: 2-nitropropane]]
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<jmolCheckbox>
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[[Category: 2-nitropropane dioxygenase]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gj/2gjl_consurf.spt"</scriptWhenChecked>
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[[Category: fmn]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:01:18 2008''
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</jmolCheckbox>
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</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=2gjl ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Pseudomonas aeruginosa PAO1]]
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[[Category: Suh SW]]

Current revision

Crystal Structure of 2-nitropropane dioxygenase

PDB ID 2gjl

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