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1hqi

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(New page: 200px<br /><applet load="1hqi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hqi" /> '''COMPONENT P2 FROM THE MULTICOMPONENT PHENOL ...)
Current revision (11:34, 27 March 2024) (edit) (undo)
 
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[[Image:1hqi.gif|left|200px]]<br /><applet load="1hqi" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hqi" />
 
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'''COMPONENT P2 FROM THE MULTICOMPONENT PHENOL HYDROXYLASE, NMR, 11 STRUCTURES'''<br />
 
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==Overview==
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==COMPONENT P2 FROM THE MULTICOMPONENT PHENOL HYDROXYLASE, NMR, 11 STRUCTURES==
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Phenol hydroxylase from Pseudomonas sp. CF600 is a member of a family of, binuclear iron-center-containing multicomponent oxygenases, which, catalyzes the conversion of phenol and some of its methyl-substituted, derivatives to catechol. In addition to a reductase component which, transfers electrons from NADH, optimal turnover of the hydroxylase, requires P2, a protein containing 90 amino acids which is readily resolved, from the other components. The three-dimensional solution structure of P2, has been solved by 3D heteronuclear NMR spectroscopy. On the basis of 1206, experimental constraints, including 1060 distance constraints obtained, from NOEs, 70 phi dihedral angle constraints, 42 psi dihedral angle, constraints, and 34 hydrogen bond constraints, a total of 12 converged, structures were obtained. The atomic root mean square deviation for the 12, converged structure with respect to the mean coordinates is 2.48 A for the, backbone atoms and 3.85 A for all the heavy atoms. This relatively large, uncertainty can be ascribed to conformational flexibility and exchange., The molecular structure of P2 is composed of three helices, six, antiparallel beta-strands, one beta-hairpin, and some less ordered, regions. This is the first structure among the known multicomponent, oxygenases. On the basis of the three-dimensional structure of P2, sequence comparisons with similar proteins from other multicomponent, oxygenases suggested that all of these proteins may have a conserved, structure in the core regions.
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<StructureSection load='1hqi' size='340' side='right'caption='[[1hqi]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1hqi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._CF600 Pseudomonas sp. CF600]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HQI FirstGlance]. <br>
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1HQI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Active as [http://en.wikipedia.org/wiki/Phenol_2-monooxygenase Phenol 2-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.7 1.14.13.7] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HQI OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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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=1hqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hqi OCA], [https://pdbe.org/1hqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hqi RCSB], [https://www.ebi.ac.uk/pdbsum/1hqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hqi ProSAT]</span></td></tr>
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==Reference==
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</table>
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Solution structure of phenol hydroxylase protein component P2 determined by NMR spectroscopy., Qian H, Edlund U, Powlowski J, Shingler V, Sethson I, Biochemistry. 1997 Jan 21;36(3):495-504. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9012665 9012665]
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== Function ==
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[[Category: Phenol 2-monooxygenase]]
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[https://www.uniprot.org/uniprot/DMPM_PSEUF DMPM_PSEUF] Catabolizes phenol, and some of its methylated derivatives. P2 is required for growth on phenol, and for in vitro phenol hydroxylase activity.
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[[Category: Pseudomonas sp.]]
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== Evolutionary Conservation ==
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[[Category: Single protein]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Qian, H.]]
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Check<jmol>
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[[Category: Sethon, I.]]
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<jmolCheckbox>
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[[Category: aromatic hydrocarbons catabolism]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hq/1hqi_consurf.spt"</scriptWhenChecked>
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[[Category: fad]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: hydroxylase]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: iron]]
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</jmolCheckbox>
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[[Category: monooxygenase flavoprotein]]
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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=1hqi ConSurf].
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[[Category: oxidoreductase]]
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<div style="clear:both"></div>
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[[Category: plasmid]]
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__TOC__
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</StructureSection>
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:44:58 2007''
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[[Category: Large Structures]]
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[[Category: Pseudomonas sp. CF600]]
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[[Category: Qian H]]
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[[Category: Sethon I]]

Current revision

COMPONENT P2 FROM THE MULTICOMPONENT PHENOL HYDROXYLASE, NMR, 11 STRUCTURES

PDB ID 1hqi

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