View source for 4wqm


==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=''>
== Structural highlights ==
<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='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='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'>[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 ==
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<ref>PMID:26309236</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4wqm" style="background-color:#fffaf0;"></div>

==See Also==
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas mendocina]]
[[Category: Acheson JF]]
[[Category: Fox BG]]