7ahd: Difference between revisions
New page: '''Unreleased structure''' The entry 7ahd is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures |
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==OpuA (E190Q) occluded== | |||
<StructureSection load='7ahd' size='340' side='right'caption='[[7ahd]], [[Resolution|resolution]] 3.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7ahd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis_subsp._lactis Lactococcus lactis subsp. lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AHD FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=BET:TRIMETHYL+GLYCINE'>BET</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7ahd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ahd OCA], [https://pdbe.org/7ahd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ahd RCSB], [https://www.ebi.ac.uk/pdbsum/7ahd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ahd ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/OPUAA_LACLA OPUAA_LACLA] Involved in a multicomponent binding-protein-dependent transport system for glycine betaine. Probably responsible for energy coupling to the transport system. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
(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. | |||
Gating by ionic strength and safety check by cyclic-di-AMP in the ABC transporter OpuA.,Sikkema HR, van den Noort M, Rheinberger J, de Boer M, Krepel ST, Schuurman-Wolters GK, Paulino C, Poolman B Sci Adv. 2020 Nov 18;6(47). pii: 6/47/eabd7697. doi: 10.1126/sciadv.abd7697., Print 2020 Nov. PMID:33208376<ref>PMID:33208376</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7ahd" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Lactococcus lactis subsp. lactis]] | |||
[[Category: Large Structures]] | |||
[[Category: Paulino C]] | |||
[[Category: Poolman B]] | |||
[[Category: Rheinberger J]] | |||
[[Category: Sikkema HR]] | |||
Latest revision as of 13:54, 15 November 2023
OpuA (E190Q) occludedOpuA (E190Q) occluded
Structural highlights
FunctionOPUAA_LACLA Involved in a multicomponent binding-protein-dependent transport system for glycine betaine. Probably responsible for energy coupling to the transport system. Publication Abstract from PubMed(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. Gating by ionic strength and safety check by cyclic-di-AMP in the ABC transporter OpuA.,Sikkema HR, van den Noort M, Rheinberger J, de Boer M, Krepel ST, Schuurman-Wolters GK, Paulino C, Poolman B Sci Adv. 2020 Nov 18;6(47). pii: 6/47/eabd7697. doi: 10.1126/sciadv.abd7697., Print 2020 Nov. PMID:33208376[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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