Three-dimensional model for the membrane domain of Escherichia coli leader peptidase based on disulfide mapping.

Abstract:

:We have mapped the interface between the two transmembrane alpha-helices in the membrane domain of the Escherichia coli enzyme leader peptidase by analyzing disulfides formed between pairs of cysteine residues introduced near their respective periplasmic ends. The interface is formed primarily from aliphatic amino acids, and the two helices appear to pack against each other in a left-handed supercoil. We suggest that disulfide mapping may be a generally applicable approach for the construction of models of helix-helix interfaces in membrane proteins.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Whitley P,Nilsson L,von Heijne G

doi

10.1021/bi00084a020

subject

Has Abstract

pub_date

1993-08-24 00:00:00

pages

8534-9

issue

33

eissn

0006-2960

issn

1520-4995

journal_volume

32

pub_type

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