Open AccessEvidence that KpsT, the ATP-binding component of an ATP-binding cassette transporter, is exposed to the periplasm and associates with polymer during translocation of the polysialic acid capsule of Escherichia coli K1
Author(s) -
Joseph M. Bliss,
Richard P. Silver
Publication year - 1997
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.179.4.1400-1403.1997
Subject(s) - periplasmic space , polysialic acid , biology , escherichia coli , biochemistry , chromosomal translocation , transporter , bacterial outer membrane , chemiosmosis , membrane transport protein , transport protein , biophysics , microbiology and biotechnology , atp synthase , enzyme , gene , cell , cell adhesion , neural cell adhesion molecule
KpsT utilizes ATP to effect translocation of the polysialic acid capsule of Escherichia coli K1. We have previously proposed a mechanistic model for the action of this protein. Here, we provide evidence to support two predictions of the model: that KpsT associates with polymer and that KpsT is accessible from the periplasmic surface of the inner membrane.