Styrene oxide isomerase: Difference between revisions
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<StructureSection load='8PNV' size='340' side='right' caption='The cryo-EM structure of the SOI-NB complex reveals that the quaternary structure of SOI consists of a homo-trimeric assembly. Each nanobody binds at the interface of two SOI protomers. Additionally, two nanobody molecules interact with each other, resulting in the formation of a dimer of trimer assemblies within the SOI-nanobody complex.. scene=''> | <StructureSection load='8PNV' size='340' side='right' caption='The cryo-EM structure of the SOI-NB complex reveals that the quaternary structure of SOI consists of a homo-trimeric assembly. Each nanobody binds at the interface of two SOI protomers. Additionally, two nanobody molecules interact with each other, resulting in the formation of a dimer of trimer assemblies within the SOI-nanobody complex.. scene=''> | ||
== Structural | == Structural features == | ||
SOI is an integral membrane protein with four transmembrane helices. It forms a novel homo-trimeric assembly with a structural fold reminiscent of ion channels. The trimeric organization, crucial for its function, is mediated by a ferric heme b prosthetic group positioned between two protomers. This ferric heme b acts as a Lewis acid, interacting with the epoxide oxygen atom of epoxide substrate, facilitating the ring-opening. | SOI is an integral membrane protein with four transmembrane helices. It forms a novel homo-trimeric assembly with a structural fold reminiscent of ion channels. The trimeric organization, crucial for its function, is mediated by a ferric heme b prosthetic group positioned between two protomers. This ferric heme b acts as a Lewis acid, interacting with the epoxide oxygen atom of epoxide substrate, facilitating the ring-opening. | ||