Using the nano discs approach at surfaces to determine the relation between substrate specificity and the conformation of cytochromes P450

DOI

Membrane bound proteins continue to be to date the most elusive molecules in nature, since they are only functional in the lipid bilayer. We have developed a method to study membrane bound proteins at surfaces using nanodiscs films. We have focused our attention to an enzyme complex producing dhurrin, since this is a model of high value pharmaceutical compounds produced by plants. In particular, we study two cytochrome P450 enzymes that catalyse the reaction of tyrosine into a dhurrin precursor. Despite being very similar in amino-acid structure, they differ largely in substrate specificity. We hypothesise that these differences are due to the specific conformation that the proteins undertake at the lipid membrane. Here we apply neutron reflection and use a series of native and mutant enzymes to corroborate our hypothesis.

Identifier
DOI https://doi.org/10.5286/ISIS.E.61001934
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/61001934
Provenance
Creator Dr Carmen Domene; Professor Marité Cárdenas Gómez; Ms Vivien Jagalski; Dr Rob Barker
Publisher ISIS Neutron and Muon Source
Publication Year 2018
Rights CC-BY Attribution 4.0 International; https://creativecommons.org/licenses/by/4.0/
OpenAccess true
Contact isisdata(at)stfc.ac.uk
Representation
Resource Type Dataset
Discipline Biology; Biomaterials; Engineering Sciences; Life Sciences; Materials Science; Materials Science and Engineering
Temporal Coverage Begin 2015-06-15T07:56:26Z
Temporal Coverage End 2015-06-17T08:00:00Z