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| ==Solution Structure of T4moC, the Rieske Ferredoxin Component of the Toluene 4-Monooxygenase Complex== | | ==Solution Structure of T4moC, the Rieske Ferredoxin Component of the Toluene 4-Monooxygenase Complex== |
| <StructureSection load='1sjg' size='340' side='right'caption='[[1sjg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | | <StructureSection load='1sjg' size='340' side='right'caption='[[1sjg]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1sjg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25411 Atcc 25411]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SJG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SJG FirstGlance]. <br> | | <table><tr><td colspan='2'>[[1sjg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_mendocina Pseudomonas mendocina]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SJG FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fqt|1fqt]]</div></td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TMOC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300 ATCC 25411])</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=1sjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sjg OCA], [https://pdbe.org/1sjg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sjg RCSB], [https://www.ebi.ac.uk/pdbsum/1sjg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sjg ProSAT]</span></td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1sjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sjg OCA], [http://pdbe.org/1sjg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sjg RCSB], [http://www.ebi.ac.uk/pdbsum/1sjg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sjg ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/TMOC_PSEME TMOC_PSEME]] Probable electron transfer from NADPH, via FAD and the 2Fe-2S center, to the oxygenase activity site of the enzyme. | | [https://www.uniprot.org/uniprot/TMOC_PSEME TMOC_PSEME] Probable electron transfer from NADPH, via FAD and the 2Fe-2S center, to the oxygenase activity site of the enzyme. |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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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=1sjg ConSurf]. | | </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=1sjg ConSurf]. |
| <div style="clear:both"></div> | | <div style="clear:both"></div> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Toluene 4-monooxygenase, a four-protein complex from Pseudomonas mendocina KR1, catalyzes the NADH- and O(2)-dependent hydroxylation of toluene to form p-cresol. The solution structure of the 112-amino-acid Rieske ferredoxin component, T4moC, was determined from 2D and 3D (1)H, (13)C, and (15)N NMR data. The structural model was refined through simulated annealing by molecular dynamics in torsion angle space with input from 1650 experimental restraints, including 1264 inter-proton distance restraints obtained from NOEs, 247 non-redundant intra-residue NOEs, 26 hydrogen bond restraints, and 113 dihedral angle ( phi, psi) restraints. The 20 calculated conformers that best satisfied the input restraints were submitted to refinement in explicit solvent to improve the stereochemical quality. With exclusion of ill-defined N- and C-terminal segments (Ser2; His111-Ser112) and residues near to the [2Fe-2S] cluster, the atomic root mean square deviation for the 20 conformers with respect to the mean coordinates was 1.09 A for the backbone and 1.60 A for all non-hydrogen atoms. The T4moC structure consists of 10 beta-strands arranged in the three anti-parallel beta-sheet topology observed in all Rieske [2Fe-2S] domain proteins. The S(gamma) of Cys45 and Cys64 and the N(delta1) of His47 and His67 provide the ligands to the [2Fe-2S] cluster of T4moC. (1)H-(15)N HSQC measurements show that both His47-N(epsilon2) and His67-N(epsilon2) are protonated at the pH of the NMR experiments. Comparisons are made between the present NMR structure, previous paramagnetic NMR studies of T4moC, and the X-ray structures of other members of the Rieske protein family.
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| Solution structure of T4moC, the Rieske ferredoxin component of the toluene 4-monooxygenase complex.,Skjeldal L, Peterson FC, Doreleijers JF, Moe LA, Pikus JD, Westler WM, Markley JL, Volkman BF, Fox BG J Biol Inorg Chem. 2004 Dec;9(8):945-53. Epub 2004 Sep 25. PMID:15452777<ref>PMID:15452777</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 1sjg" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Ferredoxin 3D structures|Ferredoxin 3D structures]] | | *[[Ferredoxin 3D structures|Ferredoxin 3D structures]] |
| *[[Monooxygenase 3D structures|Monooxygenase 3D structures]] | | *[[Monooxygenase 3D structures|Monooxygenase 3D structures]] |
| == References ==
| |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Atcc 25411]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Doreleijers, J F]] | | [[Category: Pseudomonas mendocina]] |
| [[Category: Fox, B G]] | | [[Category: Doreleijers JF]] |
| [[Category: Markley, J L]] | | [[Category: Fox BG]] |
| [[Category: Moe, L A]] | | [[Category: Markley JL]] |
| [[Category: Peterson, F C]] | | [[Category: Moe LA]] |
| [[Category: Pikus, J D]] | | [[Category: Peterson FC]] |
| [[Category: Skjeldal, L]] | | [[Category: Pikus JD]] |
| [[Category: Volkman, B F]] | | [[Category: Skjeldal L]] |
| [[Category: Westler, W M]] | | [[Category: Volkman BF]] |
| [[Category: Electron transport]]
| | [[Category: Westler WM]] |
| [[Category: Ferredoxin]]
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| [[Category: Pfam pf00355]]
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