View source for 4p1b


==CRYSTAL STRUCTURE OF THE TOLUENE 4-MONOOXYGENASE HYDROXYLASE-FERREDOXIN C7S E16C C84A C85A VARIANT ELECTRON-TRANSFER COMPLEX==
<StructureSection load='4p1b' size='340' side='right'caption='[[4p1b]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4p1b]] is a 8 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=4P1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P1B 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]] 2.05&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=4p1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p1b OCA], [https://pdbe.org/4p1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p1b RCSB], [https://www.ebi.ac.uk/pdbsum/4p1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p1b ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TMOA_ECTME TMOA_ECTME] 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:1885512, PubMed:19290655, PubMed:19705873, PubMed:2019563). Also able to convert benzene to phenol, catechol, and 1,2,3-trihydroxybenzene by successive hydroxylations (PubMed:15240250).<ref>PMID:15240250</ref> <ref>PMID:1885512</ref> <ref>PMID:19290655</ref> <ref>PMID:19705873</ref> <ref>PMID:2019563</ref> 
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== Publication Abstract from PubMed ==
Productive biomolecular recognition requires exquisite control of affinity and specificity. Accordingly, nature has devised many strategies to achieve proper binding interactions. Bacterial multicomponent monooxygenases provide a fascinating example, where a diiron hydroxylase must reversibly interact with both ferredoxin and catalytic effector in order to achieve electron transfer and O2 activation during catalysis. Because these two accessory proteins have distinct structures, and because the hydroxylase-effector complex covers the entire surface closest to the hydroxylase diiron centre, how ferredoxin binds to the hydroxylase has been unclear. Here we present high-resolution structures of toluene 4-monooxygenase hydroxylase complexed with its electron transfer ferredoxin and compare them with the hydroxylase-effector structure. These structures reveal that ferredoxin or effector protein binding produce different arrangements of conserved residues and customized interfaces on the hydroxylase in order to achieve different aspects of catalysis.

Structural basis for biomolecular recognition in overlapping binding sites in a diiron enzyme system.,Acheson JF, Bailey LJ, Elsen NL, Fox BG Nat Commun. 2014 Sep 24;5:5009. doi: 10.1038/ncomms6009. PMID:25248368<ref>PMID:25248368</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4p1b" style="background-color:#fffaf0;"></div>

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