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ABC Transporters: Exporter01:31

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ATP-binding cassette or ABC transporter is the largest superfamily of integral membrane proteins. The transporters have transmembrane-binding domains (TMDs) and nucleotide-binding domains (NBDs). The TMDs are specific to their substrates, whereas the NBDs are similar to engines that complete ATP hydrolysis to complete the substrate transport. They can be full transporters consisting of two TMDs and NBDs, half transporters with one TMD and NBD, while some encoded with a single TMD or NBD are...
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Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time
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Unexplored Nucleotide Binding Modes for the ABC Exporter MsbA.

Hundeep Kaur1, Bárbara Abreu2, Dmitry Akhmetzyanov3

  • 1Institute for Biophysical Chemistry & Centre for Biomolecular Magnetic Resonance , Goethe-University Frankfurt , 60438 Frankfurt , Germany.

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|October 6, 2018
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Summary

The ABC transporter MsbA binds nucleotides at an additional site near the Q-loop and His-Switch, crucial for its coupled ATPase and reverse adenylate kinase activities. This discovery clarifies structural mechanisms of nucleotide binding in ABC proteins.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Membrane Proteins

Background:

  • ATP-binding cassette (ABC) transporter MsbA functions as an ATP-driven lipid-A flippase.
  • MsbA belongs to the ABC protein superfamily, utilizing nucleotide-binding domains (NBDs) for ATP hydrolysis.
  • MsbA recently demonstrated a dual catalytic role, performing both ATP hydrolysis and a reverse adenylate kinase (rAK)-like reaction.

Purpose of the Study:

  • To investigate the structural basis of nucleotide binding in MsbA.
  • To elucidate the mechanism of the coupled ATPase-rAK activity.
  • To characterize nucleotide interactions within MsbA's catalytic cycle.

Main Methods:

  • Solid-state NMR (conventional and DNP-enhanced)
  • Pulsed Electron Paramagnetic Resonance (EPR) spectroscopy
  • Molecular Dynamics (MD) simulations

Main Results:

  • Identified an additional nucleotide-binding site near the Q-loop and His-Switch.
  • Demonstrated that this site does not interfere with essential metal ion coordination (using Mn2+ as a Mg2+ substitute).
  • MD simulations corroborated experimental findings, detailing nucleotide location, orientation, and binding modes.

Conclusions:

  • The newly identified nucleotide-binding site is integral to MsbA's coupled ATPase-rAK mechanism.
  • Structural insights into MsbA's nucleotide binding advance understanding of ABC transporter function.
  • This study provides a detailed mechanistic view of nucleotide and metal ion interactions in MsbA catalysis.