ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer.

By Paul C. Smith, N. Karpowich, L. Millen, Jonathan Moody, J. Rosen, P. Thomas, J. Hunt. Molecules and Cells, 2002

794 citations recorded by the source corpus.

Subfields: Infectious Diseases, Nutrition and Dietetics, Oncology

View Paper: https://www.semanticscholar.org/paper/dfea3f2f0cbe8fd79389e69fb3f0c93cc2dc6107

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In Nutrition and Dietetics

1. E. Dassa
2. C. Orelle
3. A. Davidson
4. Jue Chen
5. F. Sharom

In Oncology

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2. C. Orelle
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Citations in the corpus

• Inwardly rectifying potassium channels: their structure, function, and physiological roles. (2010, methodology): “Homology models of the three-dimensional structure of NBDs of SUR2A and SUR2B (855, 857) were made with using the monomeric structure of HisP and the ATP-mediated dimer structure of MJ0796 (292, 735).”
• ABC transporters: The power to change (2009, methodology): “This arrangement was subsequently observed with isolated transporter ABC subunit”
• Structure, Function, and Evolution of Bacterial ATP-Binding Cassette Systems (2008, methodology): “In addition to nucleotide binding, the conserved histidine residue also contacts residues across the dimer interface in the Walker A motif and the D loop, a conserved sequence following the Walker B motif, suggestive of a tight coupling between ATP binding and formation of the dimer (68, 206, 457, 5”
• KATP channels as molecular sensors of cellular metabolism (2006, background): “In bacterial NBFs, dimerization is favoured by the presence of nucleotide, and ATP hydrolysis occurs in a cooperative manne”
• Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins. (2006, background): “As mentioned earlier, in most ABC NBDs, there is a Glu residue immediately following the Walker B motif that serves as a catalytic base for cleavage of the -phosphate group (345, 472, 515).”
• Cohesin: its roles and mechanisms. (2009, background): “Like Rad50 (61) and an ABC ATPase transporter (156), the Smc1 NBD crystallizes as a dimer in the presence of the slowly hydrolysable ATP analog ATPγS (Figure 1c).”
• ABC multidrug transporters: structure, function and role in chemoresistance. (2008, background): “These NBDs form a stable dimer in the presence of ATP when the catalytic activity is inactivated by mutation [36,37].”
• The ABC protein turned chloride channel whose failure causes cystic fibrosis (2006, background): “, and by crystal structures that showed rotationally symmetric ‘head-to-tail’ NBD homodimer”