Mapping the lipid-exposed surfaces of membrane proteins

Isaiah T. Arkin, Kevin R. MacKenzie, Lillian Fisher, Saburo Aimoto, Donald M. Engelman, Steven O. Smith*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

19 Scopus citations

Abstract

Phospholamban forms a stable complex of five long transmembrane helices. We show that the relative rotational orientation of the helices in the pentameric complex can be distinguished by S-H to S-D exchange of cysteine sulphydryl groups located in the transmembrane segment of the protein and exposed to the lipid environment. Of the three cysteine residues in phospholamban, two residues (Cys 36 and Cys 46) are oriented towards the helix interface and protected from exchange, while the third cysteine (Cys 41) is oriented towards the lipid interface and undergoes exchange with water diffused into the bilayer. Distinguishing the external and internal faces of a membrane protein by sulphydryl exchange provides a general approach for determining the three-dimensional fold of membrane proteins and enhances model building efforts to generate high-resolution structures.

Original languageAmerican English
Pages (from-to)240-243
Number of pages4
JournalNature Structural Biology
Volume3
Issue number3
DOIs
StatePublished - 1996
Externally publishedYes

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