2gjl

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[[Image:2gjl.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of 2-nitropropane dioxygenase==
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|PDB= 2gjl |SIZE=350|CAPTION= <scene name='initialview01'>2gjl</scene>, resolution 2.000&Aring;
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<StructureSection load='2gjl' size='340' side='right'caption='[[2gjl]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>
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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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|ACTIVITY= <span class='plainlinks'>[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] </span>
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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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|GENE=
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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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|DOMAIN=
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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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|RELATEDENTRY=[[2gjn|2GJN]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gjl OCA], [http://www.ebi.ac.uk/pdbsum/2gjl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gjl RCSB]</span>
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== Function ==
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}}
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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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== Evolutionary Conservation ==
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'''Crystal Structure of 2-nitropropane dioxygenase'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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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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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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<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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==About this Structure==
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</jmolCheckbox>
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2GJL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GJL OCA].
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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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==Reference==
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== References ==
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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://www.ncbi.nlm.nih.gov/pubmed/16682407 16682407]
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<references/>
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[[Category: 2-nitropropane dioxygenase]]
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__TOC__
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[[Category: Pseudomonas aeruginosa]]
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</StructureSection>
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Suh, S W.]]
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[[Category: Pseudomonas aeruginosa PAO1]]
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[[Category: 2-nitropropane]]
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[[Category: Suh SW]]
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[[Category: fmn]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:17:32 2008''
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Current revision

Crystal Structure of 2-nitropropane dioxygenase

PDB ID 2gjl

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