3ihm

<table><tr><td colspan='2'>[[3ihm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IHM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IHM FirstGlance]. <br>

</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=3ihm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ihm OCA], [https://pdbe.org/3ihm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ihm RCSB], [https://www.ebi.ac.uk/pdbsum/3ihm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ihm ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Styrene monooxygenase (SMO) is a two-component flavoprotein monooxygenase that transforms styrene to styrene oxide in the first step of the styrene catabolic and detoxification pathway of Pseudomonas putida S12. The crystal structure of the N-terminally histidine-tagged epoxidase component of this system, NSMOA, determined to 2.3 A resolution, indicates the enzyme exists as a homodimer in which each monomer forms two distinct domains. The overall architecture is most similar to that of p-hydroxybenzoate hydroxylase (PHBH), although there are some significant differences in secondary structure. Structural comparisons suggest that a large cavity open to the surface forms the FAD binding site. At the base of this pocket is another cavity that likely represents the styrene binding site. Flavin binding and redox equilibria are tightly coupled such that reduced FAD binds apo NSMOA approximately 8000 times more tightly than the oxidized coenzyme. Equilibrium fluorescence and isothermal titration calorimetry data using benzene as a substrate analogue indicate that the oxidized flavin and substrate analogue binding equilibria of NSMOA are linked such that the binding affinity of each is increased by 60-fold when the enzyme is saturated with the other. A much weaker approximately 2-fold positive cooperative interaction is observed for the linked binding equilibria of benzene and reduced FAD. The low affinity of the substrate analogue for the reduced FAD complex of NSMOA is consistent with a preferred reaction order in which flavin reduction and reaction with oxygen precede the binding of styrene, identifying the apoenzyme structure as the key catalytic resting state of NSMOA poised to bind reduced FAD and initiate the oxygen reaction.

Structure and ligand binding properties of the epoxidase component of styrene monooxygenase .,Ukaegbu UE, Kantz A, Beaton M, Gassner GT, Rosenzweig AC Biochemistry. 2010 Mar 2;49(8):1678-88. PMID:20055497<ref>PMID:20055497</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Bacillus fluorescens putidus flugge 1886]]

[[Category: Gassner, G]]

[[Category: Rosenzweig, A C]]

[[Category: Ukaegbu, U E]]

[[Category: Anti-parallel beta strand]]

[[Category: Rossmann fold]]