Mechanistic determinants of the directionality and energetics of active export by a heterodimeric ABC transporter

Grossmann, Nina; Vakkasoglu, Ahmet S.; Hulpke, Sabine; Abele, Rupert; Gaudet, Rachelle; Tampé, Robert

doi:10.1038/ncomms6419

Title: Mechanistic determinants of the directionality and energetics of active export by a heterodimeric ABC transporter

Journal Article · Fri Nov 07 00:00:00 EST 2014 · Nature Communications

DOI:https://doi.org/10.1038/ncomms6419· OSTI ID:1163789

Grossmann, Nina ^[1]; Vakkasoglu, Ahmet S. ^[2]; Hulpke, Sabine ^[1]; Abele, Rupert ^[1]; Gaudet, Rachelle ^[2]; Tampé, Robert ^[1]

Goethe Univ., Frankfurt (Germany)
Harvard Univ., Cambridge, MA (United States)

The ATP-binding cassette (ABC) transporter associated with antigen processing (TAP) participates in immune surveillance by moving proteasomal products into the endoplasmic reticulum (ER) lumen for major histocompatibility complex class I loading and cell surface presentation to cytotoxic T cells. Here we delineate the mechanistic basis for antigen translocation. Notably, TAP works as a molecular diode, translocating peptide substrates against the gradient in a strict unidirectional way. We reveal the importance of the D-loop at the dimer interface of the two nucleotide-binding domains (NBDs) in coupling substrate translocation with ATP hydrolysis and defining transport vectoriality. Substitution of the converved aspartate, which coordinates the ATP-binding site, decreases NBD dimerization affinity and turns the unidirectional primary active pump into a passive bidirectional nucleotide-gated facilitator. Thus, ATP hydrolysis is not required for translocation per se, but is essential for both active and unidirectional transport. As a result, our data provide detailed mechanistic insight into how heterodimeric ABC exporters operate.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: USDOE

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1163789

Journal Information:: Nature Communications, Vol. 5; ISSN 2041-1723

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 74 works

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