Evidence 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.

AUTOR(ES)

Bliss, J M

RESUMO

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.

Documentos Relacionados

• Identification of two genes, kpsM and kpsT, in region 3 of the polysialic acid gene cluster of Escherichia coli K1.
• A Novel Bacterial ATP-Binding Cassette Transporter System That Allows Uptake of Macromolecules
• Trapping the transition state of an ATP-binding cassette transporter: Evidence for a concerted mechanism of maltose transport
• Vanadate-catalyzed photocleavage of the signature motif of an ATP-binding cassette (ABC) transporter
• An ATP-Binding Cassette Transporter GhWBC1 from Elongating Cotton Fibers1