A snapshot of nature's favorite pump

Philip J. Thomas; John F. Hunt

doi:10.1038/nsb1101-920

A snapshot of nature's favorite pump

Philip J. Thomas, John F. Hunt

Research output: Contribution to journal › Short survey › peer-review

25 Scopus citations

Abstract

The 4.5 Å map of the MsbA protein, a putative lipid A transporter from Escherichia coli, provides the first detailed structural model for the transmembrane domain and cytoplasmic 'loops' of an ABC transporter and the geometric relationship of these regions to the ATP-binding cassette motor domain. Based on this structure, specific hypotheses for the mechanics of the pump can now be formulated and tested.

Original language	English (US)
Pages (from-to)	920-923
Number of pages	4
Journal	Nature Structural Biology
Volume	8
Issue number	11
DOIs	https://doi.org/10.1038/nsb1101-920
State	Published - 2001

ASJC Scopus subject areas

Structural Biology
Biochemistry
Genetics

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10.1038/nsb1101-920

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abstract = "The 4.5 {\AA} map of the MsbA protein, a putative lipid A transporter from Escherichia coli, provides the first detailed structural model for the transmembrane domain and cytoplasmic 'loops' of an ABC transporter and the geometric relationship of these regions to the ATP-binding cassette motor domain. Based on this structure, specific hypotheses for the mechanics of the pump can now be formulated and tested.",

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AB - The 4.5 Å map of the MsbA protein, a putative lipid A transporter from Escherichia coli, provides the first detailed structural model for the transmembrane domain and cytoplasmic 'loops' of an ABC transporter and the geometric relationship of these regions to the ATP-binding cassette motor domain. Based on this structure, specific hypotheses for the mechanics of the pump can now be formulated and tested.

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A snapshot of nature's favorite pump

Abstract

ASJC Scopus subject areas

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