- EMDB-11785: OpuA inward-facing in the presence of glycine betaine -
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Basic information
Entry
Database: EMDB / ID: EMD-11785
Title
OpuA inward-facing in the presence of glycine betaine
Map data
Sample
Complex: OpuA inward facing in the presence of glycine betaine
Protein or peptide: OpuABC
Protein or peptide: OpuAA
Function / homology
Function and homology information
amine transmembrane transporter activity / ABC-type quaternary amine transporter / ABC-type quaternary ammonium compound transporting activity / carnitine transmembrane transporter activity / glycine betaine transport / choline transport / peptide transport / amino acid transport / ATP-binding cassette (ABC) transporter complex / protein transport ...amine transmembrane transporter activity / ABC-type quaternary amine transporter / ABC-type quaternary ammonium compound transporting activity / carnitine transmembrane transporter activity / glycine betaine transport / choline transport / peptide transport / amino acid transport / ATP-binding cassette (ABC) transporter complex / protein transport / ATP hydrolysis activity / ATP binding / membrane Similarity search - Function
Glycine betaine transport ATP-binding subunit / ABC-type glycine betaine transport system, substrate-binding domain / Substrate binding domain of ABC-type glycine betaine transport system / ABC transporter type 1, transmembrane domain MetI-like / MetI-like superfamily / Binding-protein-dependent transport system inner membrane component / ABC transporter integral membrane type-1 domain profile. / CBS domain superfamily / CBS domain / CBS domain ...Glycine betaine transport ATP-binding subunit / ABC-type glycine betaine transport system, substrate-binding domain / Substrate binding domain of ABC-type glycine betaine transport system / ABC transporter type 1, transmembrane domain MetI-like / MetI-like superfamily / Binding-protein-dependent transport system inner membrane component / ABC transporter integral membrane type-1 domain profile. / CBS domain superfamily / CBS domain / CBS domain / CBS domain profile. / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase Similarity search - Domain/homology
Quaternary amine transport ATP-binding protein / ABC transporter permease/substrate binding protein / Glycine betaine transport ATP-binding protein OpuAA Similarity search - Component
Netherlands Organisation for Scientific Research (NWO)
740.018.016
Netherlands
Netherlands Organisation for Scientific Research (NWO)
722.017.001
Netherlands
Citation
Journal: Sci Adv / Year: 2020 Title: Gating by ionic strength and safety check by cyclic-di-AMP in the ABC transporter OpuA. Authors: Hendrik R Sikkema / Marco van den Noort / Jan Rheinberger / Marijn de Boer / Sabrina T Krepel / Gea K Schuurman-Wolters / Cristina Paulino / Bert Poolman / Abstract: (Micro)organisms are exposed to fluctuating environmental conditions, and adaptation to stress is essential for survival. Increased osmolality (hypertonicity) causes outflow of water and loss of ...(Micro)organisms are exposed to fluctuating environmental conditions, and adaptation to stress is essential for survival. Increased osmolality (hypertonicity) causes outflow of water and loss of turgor and is dangerous if the cell is not capable of rapidly restoring its volume. The osmoregulatory adenosine triphosphate-binding cassette transporter OpuA restores the cell volume by accumulating large amounts of compatible solute. OpuA is gated by ionic strength and inhibited by the second messenger cyclic-di-AMP, a molecule recently shown to affect many cellular processes. Despite the master regulatory role of cyclic-di-AMP, structural and functional insights into how the second messenger regulates (transport) proteins on the molecular level are lacking. Here, we present high-resolution cryo-electron microscopy structures of OpuA and in vitro activity assays that show how the osmoregulator OpuA is activated by high ionic strength and how cyclic-di-AMP acts as a backstop to prevent unbridled uptake of compatible solutes.
History
Deposition
Sep 24, 2020
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Header (metadata) release
Nov 25, 2020
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Map release
Nov 25, 2020
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Update
Dec 2, 2020
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Current status
Dec 2, 2020
Processing site: PDBe / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
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