caa a22 4500 445325461 CHVBK 20180317142719.0 cr unu---uuuuu 170323e20110901xx s 000 0 eng 10.1007/s10858-011-9543-z doi (NATIONALLICENCE)springer-10.1007/s10858-011-9543-z Siderocalin Q83 exhibits differential slow dynamics upon ligand binding [Elektronische Daten] [Nicolas Coudevylle, Leonhard Geist, Matthias Hoetzinger, Martin Tollinger, Robert Konrat] Siderocalin Q83 is a small soluble protein that has the ability to bind two different ligands (enterobactin and arachidonic acid) simultaneously in two distinct binding sites. Here we report that Q83 exhibits an intriguing dynamic behavior. In its free form, the protein undergoes significant micro-to-millisecond dynamics. When binding arachidonic acid, the motions of the arachidonic acid binding site are quenched while the dynamics at the enterobactin binding site increases. Reciprocally, enterobactin binding to Q83 quenches the motions at the enterobactin binding site and increases the slow dynamics at the arachidonic acid binding site. Additionally, in the enterobactin-bound state, the excited state of the arachidonic acid binding site resembles the arachidonic acid-bound state. These observations strongly suggest an allosteric regulation where binding of one ligand enhances the affinity of Q83 for the other one. Additionally, our data strengthen the emerging view of proteins as dynamic ensembles interconverting between different sub-states with distinct functionalities. Springer Science+Business Media B.V., 2011 Siderocalin nationallicence Enterobactin nationallicence Arachidonic acid nationallicence Ligand binding nationallicence NMR nationallicence CPMG nationallicence NMR : Nuclear magnetic resonance nationallicence CPMG : Carr Purcell Meiboom Gill nationallicence AA : Arachidonic acid nationallicence DTT : Dithiotreitol nationallicence Coudevylle Nicolas Department of Computational and Structural Biology, Max F. Perutz Laboratories, Campus Vienna Biocenter 5, 1030, Vienna, Austria aut Geist Leonhard Department of Computational and Structural Biology, Max F. Perutz Laboratories, Campus Vienna Biocenter 5, 1030, Vienna, Austria aut Hoetzinger Matthias Department of Computational and Structural Biology, Max F. Perutz Laboratories, Campus Vienna Biocenter 5, 1030, Vienna, Austria aut Tollinger Martin Institute of Organic Chemistry, Leopold-Franzens University Innsbruck, Innrain 52a, 6020, Innsbruck, Austria aut Konrat Robert Department of Computational and Structural Biology, Max F. Perutz Laboratories, Campus Vienna Biocenter 5, 1030, Vienna, Austria aut Journal of Biomolecular NMR Springer Netherlands 51/1-2(2011-09-01), 83-88 0925-2738 51:1-2<83 2011 51 10858 https://doi.org/10.1007/s10858-011-9543-z text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-011-9543-z text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Coudevylle Nicolas Department of Computational and Structural Biology, Max F. Perutz Laboratories, Campus Vienna Biocenter 5, 1030, Vienna, Austria aut NATIONALLICENCE 700 1- Geist Leonhard Department of Computational and Structural Biology, Max F. Perutz Laboratories, Campus Vienna Biocenter 5, 1030, Vienna, Austria aut NATIONALLICENCE 700 1- Hoetzinger Matthias Department of Computational and Structural Biology, Max F. Perutz Laboratories, Campus Vienna Biocenter 5, 1030, Vienna, Austria aut NATIONALLICENCE 700 1- Tollinger Martin Institute of Organic Chemistry, Leopold-Franzens University Innsbruck, Innrain 52a, 6020, Innsbruck, Austria aut NATIONALLICENCE 700 1- Konrat Robert Department of Computational and Structural Biology, Max F. Perutz Laboratories, Campus Vienna Biocenter 5, 1030, Vienna, Austria aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 51/1-2(2011-09-01), 83-88 0925-2738 51:1-2<83 2011 51 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer