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Structure paper

TitleGating by ionic strength and safety check by cyclic-di-AMP in the ABC transporter OpuA.
Journal, issue, pagesSci Adv, Vol. 6, Issue 47, Year 2020
Publish dateNov 18, 2020
AuthorsHendrik R Sikkema / Marco van den Noort / Jan Rheinberger / Marijn de Boer / Sabrina T Krepel / Gea K Schuurman-Wolters / Cristina Paulino / Bert Poolman /
PubMed 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.
External linksSci Adv / PubMed:33208376 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 4.5 Å
Structure data

11782

7ahc

EMDB-11782, PDB-7ahc:
OpuA apo inward-facing
Method: EM (single particle) / Resolution: 3.3 Å

11783

7ahd

EMDB-11783, PDB-7ahd:
OpuA (E190Q) occluded
Method: EM (single particle) / Resolution: 3.4 Å

11784

7ahe

EMDB-11784, PDB-7ahe:
OpuA inhibited inward facing
Method: EM (single particle) / Resolution: 4.1 Å

EMDB-11785:
OpuA inward-facing in the presence of glycine betaine
Method: EM (single particle) / Resolution: 4.5 Å

11786

7ahh

EMDB-11786, PDB-7ahh:
OpuA inhibited inward-facing, SBD docked
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-BET:
TRIMETHYL GLYCINE / Trimethylglycine

ChemComp-2BA:
(2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

Source
  • lactococcus lactis subsp. lactis (lactic acid bacteria)
KeywordsMEMBRANE PROTEIN / osmoregulation / ABC-transporter / glycine betaine uptake system / cyclic-di-AMP

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