Carbene Footprinting Reveals Binding Interfaces of a Multimeric Membrane‐Spanning Protein

Manzi, Lucio, Barrow, Andrew S, Hopper, Jonathan TS, Kaminska, Renata, Kleanthous, Colin, Robinson, Carol V, Moses, John E, Oldham, Neil J (November 2017) Carbene Footprinting Reveals Binding Interfaces of a Multimeric Membrane‐Spanning Protein. Angewandte Chemie International Edition, 129 (47). pp. 15069-15073. ISSN 0044-8249

DOI: 10.1002/ange.201708254


Mapping the interaction sites between membrane‐spanning proteins is a key challenge in structural biology. In this study a carbene‐footprinting approach was developed and applied to identify the interfacial sites of a trimeric, integral membrane protein, OmpF, solubilised in micelles. The diazirine‐based footprinting probe is effectively sequestered by, and incorporated into, the micelles, thus leading to efficient labelling of the membrane‐spanning regions of the protein upon irradiation at 349 nm. Areas associated with protein–protein interactions between the trimer subunits remained unlabelled, thus revealing their location.

Item Type: Paper
Subjects: organs, tissues, organelles, cell types and functions > tissues types and functions > transport > membrane transport
CSHL Authors:
Communities: CSHL labs > Moses lab
SWORD Depositor: CSHL Elements
Depositing User: CSHL Elements
Date: 20 November 2017
Date Deposited: 03 Oct 2023 20:49
Last Modified: 03 Oct 2023 20:49
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