8b5e: Difference between revisions
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==Exploring the ligand binding and conformational dynamics of receptor domain 1 of the ABC transporter GlnPQ== | |||
<StructureSection load='8b5e' size='340' side='right'caption='[[8b5e]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8b5e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8B5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8B5E FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</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=8b5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8b5e OCA], [https://pdbe.org/8b5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8b5e RCSB], [https://www.ebi.ac.uk/pdbsum/8b5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8b5e ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A2X0R690_9LACT A0A2X0R690_9LACT] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The adenosine triphosphate (ATP)-binding cassette (ABC) importer GlnPQ from Lactococcus lactis has two sequential covalently linked substrate-binding domains (SBDs), which capture the substrates and deliver them to the translocon. The two SBDs differ in their ligand specificities, binding affinities and the distance to the transmembrane domain; interestingly, both SBDs can bind their ligands simultaneously without affecting each other. In this work, we studied the binding of ligands to both SBDs using X-ray crystallography and molecular dynamics simulations. We report three high-resolution structures of SBD1, namely, the wild-type SBD1 with bound asparagine or arginine, and E184D SBD1 with glutamine bound. Molecular dynamics (MD) simulations provide a detailed insight into the dynamics associated with open-closed transitions of the SBDs. | |||
Exploring the Ligand Binding and Conformational Dynamics of the Substrate-Binding Domain 1 of the ABC Transporter GlnPQ.,Nemchinova M, Schuurman-Wolters GK, Whittaker JJ, Arkhipova V, Marrink SJ, Poolman B, Guskov A J Phys Chem B. 2024 Aug 15;128(32):7822-7832. doi: 10.1021/acs.jpcb.4c02662. Epub , 2024 Aug 1. PMID:39090964<ref>PMID:39090964</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Guskov | <div class="pdbe-citations 8b5e" style="background-color:#fffaf0;"></div> | ||
[[Category: Whittaker | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Lactococcus lactis]] | |||
[[Category: Large Structures]] | |||
[[Category: Guskov A]] | |||
[[Category: Whittaker J]] | |||
Latest revision as of 08:50, 4 September 2024
Exploring the ligand binding and conformational dynamics of receptor domain 1 of the ABC transporter GlnPQExploring the ligand binding and conformational dynamics of receptor domain 1 of the ABC transporter GlnPQ
Structural highlights
FunctionPublication Abstract from PubMedThe adenosine triphosphate (ATP)-binding cassette (ABC) importer GlnPQ from Lactococcus lactis has two sequential covalently linked substrate-binding domains (SBDs), which capture the substrates and deliver them to the translocon. The two SBDs differ in their ligand specificities, binding affinities and the distance to the transmembrane domain; interestingly, both SBDs can bind their ligands simultaneously without affecting each other. In this work, we studied the binding of ligands to both SBDs using X-ray crystallography and molecular dynamics simulations. We report three high-resolution structures of SBD1, namely, the wild-type SBD1 with bound asparagine or arginine, and E184D SBD1 with glutamine bound. Molecular dynamics (MD) simulations provide a detailed insight into the dynamics associated with open-closed transitions of the SBDs. Exploring the Ligand Binding and Conformational Dynamics of the Substrate-Binding Domain 1 of the ABC Transporter GlnPQ.,Nemchinova M, Schuurman-Wolters GK, Whittaker JJ, Arkhipova V, Marrink SJ, Poolman B, Guskov A J Phys Chem B. 2024 Aug 15;128(32):7822-7832. doi: 10.1021/acs.jpcb.4c02662. Epub , 2024 Aug 1. PMID:39090964[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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