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ATP-binding cassette (ABC) transporters are integral membrane proteins thatmediate the exchange of diverse substrates across membranes powered by ATPhydrolysis. We report results of coarse-grained dynamical simulations performedfor the bacterial heme transporter HmuUV. Based on the nucleotide-freestructure, we have constructed a ligand-elastic-network description for thisprotein and investigated ATP-induced conformational motions in structurallyresolved computer experiments. As we found, interactions with nucleotidesresulted in generic motions which are functional and robust. Upon binding ofATP-mimicking ligands the structure changed from a conformation in which thenucleotide-binding domains formed an open shape, to a conformation in whichthey were found in tight contact and the transmembrane domains were rotated.The heme channel was broadened in the ligand-bound complex and the gate to thecytoplasm, which was closed in the nucleotide-free conformation, was renderedopen by a mechanism that involved tilting motions of essential transmembranehelices. Based on our findings we propose that the HmuUV transporter behaveslike a `simple' mechanical device in which, induced by binding of ATP ligands,linear motions of the nucleotide-binding domains are translated into rotationalmotions and internal tilting dynamics of the transmembrane domains that controlgating inside the heme pathway.

Nucleotide-induced conformational motions and transmembrane gating dynamics in a bacterial ABC transporter