4wqm: Difference between revisions

Latest revision as of 11:57, 13 August 2026

Structure of the toluene 4-monooxygenase NADH oxidoreductase T4moF, K270S K271S variant

Structural highlights

4wqm is a 1 chain structure with sequence from Pseudomonas mendocina. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.62Å
Ligands:	BTB, FAD, FES, NI
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TMOF_ECTME Reductase component of the toluene-4-monooxygenase multicomponent enzyme system which catalyzes the O2- and NADH-dependent hydroxylation of toluene to form p-cresol (PubMed:15240250, PubMed:17964805). Ferredoxin reductase catalyzes the transfer of electrons from NADH to ferredoxin (TmoC) (PubMed:17964805).^[1] ^[2] ^[3]

Publication Abstract from PubMed

The 1.6 A crystal structure of toluene 4-monooxygenase reductase T4moF is reported. The structure includes ferredoxin, flavin, and NADH binding domains. The position of the ferredoxin domain relative to the other two domains represents a new configuration for the iron-sulfur flavoprotein family. Close contacts between the C8 methyl group of FAD and [2Fe-2S] ligand Cys36-O represent a plausible pathway for electron transfer between the redox cofactors. Energy-minimized docking of NADH and calculation of hinge-like motions between domains suggest how simple coordinated shifts of residues at the C-terminus of the enzyme could expose the N5 position of FAD for productive interaction with the nicotinamide ring. The domain configuration revealed by the T4moF structure provides an excellent steric and electrostatic match to the obligate electron acceptor, Rieske-type [2Fe-2S] ferredoxin T4moC. Protein-protein docking and energy minimization of the T4moFC complex indicate that T4moF [2Fe-2S] ligand Cys41 and T4moC [2Fe-2S] ligand His67, along with other electrostatic interactions between the protein partners, form the functional electron transfer interface.

Structure of T4moF, the toluene 4-monooxygenase ferredoxin oxidoreductase.,Acheson JF, Moseson H, Fox BG Biochemistry. 2015 Aug 26. PMID:26309236^[4]

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

References

↑ Tao Y, Fishman A, Bentley WE, Wood TK. Oxidation of benzene to phenol, catechol, and 1,2,3-trihydroxybenzene by toluene 4-monooxygenase of Pseudomonas mendocina KR1 and toluene 3-monooxygenase of Ralstonia pickettii PKO1. Applied and environmental microbiology. 2004 Jul 1. doi: 10.1128/AEM.70.7.3814-3820.2004. PMID: 15240250.
↑ Bailey LJ, Elsen NL, Pierce BS, Fox BG. Soluble expression and purification of the oxidoreductase component of toluene 4-monooxygenase. Protein Expr Purif. 2008 Jan;57(1):9-16. doi: 10.1016/j.pep.2007.09.007. Epub , 2007 Sep 19. PMID:17964805 doi:https://dx.doi.org/10.1016/j.pep.2007.09.007
↑ Yen KM, Karl MR. Identification of a new gene, tmoF, in the Pseudomonas mendocina KR1 gene cluster encoding toluene-4-monooxygenase. J Bacteriol. 1992 Nov;174(22):7253-61. doi: 10.1128/jb.174.22.7253-7261.1992. PMID:1429451 doi:https://dx.doi.org/10.1128/jb.174.22.7253-7261.1992
↑ Acheson JF, Moseson H, Fox BG. Structure of T4moF, the toluene 4-monooxygenase ferredoxin oxidoreductase. Biochemistry. 2015 Aug 26. PMID:26309236 doi:https://dx.doi.org/10.1021/acs.biochem.5b00692

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Tao Y, Fishman A, Bentley WE, Wood TK. Oxidation of benzene to phenol, catechol, and 1,2,3-trihydroxybenzene by toluene 4-monooxygenase of Pseudomonas mendocina KR1 and toluene 3-monooxygenase of Ralstonia pickettii PKO1. Applied and environmental microbiology. 2004 Jul 1. doi: 10.1128/AEM.70.7.3814-3820.2004. PMID: 15240250.

[2] Bailey LJ, Elsen NL, Pierce BS, Fox BG. Soluble expression and purification of the oxidoreductase component of toluene 4-monooxygenase. Protein Expr Purif. 2008 Jan;57(1):9-16. doi: 10.1016/j.pep.2007.09.007. Epub , 2007 Sep 19. PMID:17964805 doi:https://dx.doi.org/10.1016/j.pep.2007.09.007

[3] Yen KM, Karl MR. Identification of a new gene, tmoF, in the Pseudomonas mendocina KR1 gene cluster encoding toluene-4-monooxygenase. J Bacteriol. 1992 Nov;174(22):7253-61. doi: 10.1128/jb.174.22.7253-7261.1992. PMID:1429451 doi:https://dx.doi.org/10.1128/jb.174.22.7253-7261.1992

[4] Acheson JF, Moseson H, Fox BG. Structure of T4moF, the toluene 4-monooxygenase ferredoxin oxidoreductase. Biochemistry. 2015 Aug 26. PMID:26309236 doi:https://dx.doi.org/10.1021/acs.biochem.5b00692

[1]

[2]

[3]

[4]

@@ Line 1: / Line 1: @@
 ==Structure of the toluene 4-monooxygenase NADH oxidoreductase T4moF, K270S K271S variant==
-<StructureSection load='4wqm' size='340' side='right' caption='[[4wqm]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
+<StructureSection load='4wqm' size='340' side='right'caption='[[4wqm]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4wqm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WQM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WQM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4wqm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_mendocina Pseudomonas mendocina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WQM FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.62&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferredoxin--NAD(+)_reductase Ferredoxin--NAD(+) reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.1.3 1.18.1.3] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></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=4wqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wqm OCA], [http://pdbe.org/4wqm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wqm RCSB], [http://www.ebi.ac.uk/pdbsum/4wqm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wqm ProSAT]</span></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=4wqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wqm OCA], [https://pdbe.org/4wqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wqm RCSB], [https://www.ebi.ac.uk/pdbsum/4wqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wqm ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/TMOF_ECTME TMOF_ECTME] Reductase component of the toluene-4-monooxygenase multicomponent enzyme system which catalyzes the O2- and NADH-dependent hydroxylation of toluene to form p-cresol (PubMed:15240250, PubMed:17964805). Ferredoxin reductase catalyzes the transfer of electrons from NADH to ferredoxin (TmoC) (PubMed:17964805).<ref>PMID:15240250</ref> <ref>PMID:17964805</ref> <ref>PMID:1429451</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 21: @@
 ==See Also==
-*[[Monooxygenase|Monooxygenase]]
+*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Acheson, J F]]
+[[Category: Large Structures]]
-[[Category: Fox, B G]]
+[[Category: Pseudomonas mendocina]]
-[[Category: Electron-transfer]]
+[[Category: Acheson JF]]
-[[Category: Ferredoxin-nad reductase]]
+[[Category: Fox BG]]
-[[Category: Iron-sulfur]]
-[[Category: Oxidoreductase]]

4wqm: Difference between revisions

Latest revision as of 11:57, 13 August 2026

Structure of the toluene 4-monooxygenase NADH oxidoreductase T4moF, K270S K271S variant

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools