Dataset Information

Carbene footprinting reveals binding interfaces of a multimeric membrane spanning protein

ABSTRACT: Mapping the interaction sites between membrane spanning proteins is a key challenge in structural biology. Here we develop and apply carbene footprinting technology to identify the interfacial sites of a trimeric membrane protein. We show how the footprinting probe is effectively incorporated into detergent micelles leading to efficient labelling of the external membrane-spanning regions of the protein.

INSTRUMENT(S): LTQ FT

ORGANISM(S): Escherichia Coli

SUBMITTER: Lucio Manzi

LAB HEAD: Neil J. Oldham

PROVIDER: PXD007207 | Pride | 2017-09-29

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	LM_AD_OmpF_1_040816.RAW	Raw
	LM_AD_OmpF_1_CID1_040816.RAW	Raw
	LM_AD_OmpF_1_CID2_040816.RAW	Raw
	LM_AD_OmpF_2_040816.RAW	Raw
	LM_AD_OmpF_2_CID1_040816.RAW	Raw

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Carbene Footprinting Reveals Binding Interfaces of a Multimeric Membrane-Spanning Protein.

Manzi Lucio L Barrow Andrew S AS Hopper Jonathan T S JTS Kaminska Renata R Kleanthous Colin C Robinson Carol V CV Moses John E JE Oldham Neil J NJ

Angewandte Chemie (International ed. in English) 20171020 47

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 ...[more]

PMID: 28960650

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