8b5e: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 8b5e is ON HOLD
+==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]] 1.60&Aring;' 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]] 1.6&#8491;</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.
-Authors: Whittaker, J., Guskov, A.
+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>
-Description: Exploring the ligand binding and conformational dynamics of receptor domain 1 of the ABC transporter GlnPQ
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Guskov, A]]
+<div class="pdbe-citations 8b5e" style="background-color:#fffaf0;"></div>
-[[Category: Whittaker, J]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Lactococcus lactis]]
+[[Category: Large Structures]]
+[[Category: Guskov A]]
+[[Category: Whittaker J]]