Dresden 2017 – wissenschaftliches Programm

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BP: Fachverband Biologische Physik

BP 56: Protein Structure and Dynamics

BP 56.2: Vortrag

Donnerstag, 23. März 2017, 15:30–15:45, SCH A251

Molecular mechanisms of substrate binding proteins in ABC transporters — Marijn de Boer, Florence Husada, Kostas Tassis, Yusran Muthahari, Giorgos Gouridis, and •Thorben Cordes — Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 4, 9747AG Groningen, The Netherlands

ATP-binding cassette (ABC) transporters mediate unidirectional active transport of diverse substrates across membranes using ATP hydrolysis. During import in prokaryotes, specialized substrate binding proteins or domains (SBDs) at first capture a substrate for delivery to the translocator domain and subsequent transport. Different SBDs show a high structural conservation but only little sequence similarity. Their fold consists of two rigid α/β domains, which form the binding cavity, and that are connected by a (flexible) hinge. We here test the hypothesis, whether there is a relationship between the SBD hinge structure and conformational dynamics of the SBDs based on the fact that the hinge bends during the conformational transition from open unliganded to closed liganded state. For this we use single-molecule Förster resonance energy transfer (smFRET) that allows to elucidate the conformational states and dynamics of SBDs directly and with this to understand their mechanistic role for transport.[1-3]

[1] G. Gouridis et al., Nature Structural & Molecular Biology 22 (2015) 57-64. [2] F. Husada et al., Biochemical Society Transactions 43 (2015) 1041-1047. [3] J. H. M. van der Velde et al., Nature Communications 7:10144 (2016).