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Related Experiment Videos

Structure-function relationships in an anion-translocating ATPase.

H Bhattacharjee1, T Zhou, J Li

  • 1Department of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, Detroit, MI 48201, USA.

Biochemical Society Transactions
|August 30, 2000
PubMed
Summary
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The ArsAB ATPase pump in E. coli extrudes toxic arsenite and antimonite, conferring resistance. Its mechanism reveals how ATP-binding cassette transporters overcome rate-limiting steps through conformational changes.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • The ArsAB ATPase is an inner membrane efflux pump in Escherichia coli.
  • It confers resistance to arsenite and antimonite by extruding these toxic metalloids.
  • The pump comprises the catalytic ArsA subunit and the membrane-bound ArsB subunit, functioning as an ATP-binding cassette (ABC) transporter.

Purpose of the Study:

  • To elucidate the mechanism of allosteric activation of the ArsA ATPase.
  • To understand how conformational changes in ArsAB contribute to its function as an efflux pump.
  • To establish ArsAB as a model for studying the broader ABC transporter superfamily.

Main Methods:

  • Molecular genetics
  • Biochemical analyses

Related Experiment Videos

  • Structural analyses
  • Kinetic analyses
  • Stopped-flow fluorescence measurements using single-tryptophan derivatives of ArsA

    • Main Results:

    • The ArsB subunit contains 12 transmembrane segments and forms the substrate translocation pathway.
    • The ArsA subunit is a substrate-activated ATPase with two nucleotide-binding domains (NBDs), resulting from gene duplication.
    • Allosteric activation accelerates catalysis by increasing the rate of a slow isomerization between enzyme conformations, making product release rate-limiting.

    Conclusions:

    • The ArsAB pump's mechanism involves overcoming a rate-limiting isomerization step through conformational changes.
    • ArsAB serves as a valuable model for understanding the mechanistic principles of ABC transporters.
    • This study provides insights into substrate-activated ATPase mechanisms within the ABC transporter superfamily.