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Amy L. Davidson
Researcher at Purdue University
Publications - 51
Citations - 6237
Amy L. Davidson is an academic researcher from Purdue University. The author has contributed to research in topics: ATP-binding cassette transporter & ATP hydrolysis. The author has an hindex of 29, co-authored 51 publications receiving 5941 citations. Previous affiliations of Amy L. Davidson include Baylor College of Medicine & University of California, Berkeley.
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Journal ArticleDOI
Structure, Function, and Evolution of Bacterial ATP-Binding Cassette Systems
TL;DR: The availability of an increasing number of high-resolution structures has provided a valuable framework for interpretation of recent studies, and realistic models have been proposed to explain how these fascinating molecular machines use complex dynamic processes to fulfill their numerous biological functions.
Journal ArticleDOI
ATP-binding cassette transporters in bacteria.
Amy L. Davidson,Jue Chen +1 more
TL;DR: Recent advances in structural determination and functional analysis of bacterial ABC transporters have greatly increased the understanding of the molecular mechanism of transport in this transport superfamily.
Journal ArticleDOI
A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle.
TL;DR: The crystal structures of MalK, the ATPase subunit of the maltose transporter from Escherichia coli, in three different dimeric configurations suggest a regulatory mechanism for ATPase activity that may be tightly coupled to translocation.
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Crystal structure of a catalytic intermediate of the maltose transporter
TL;DR: The 2.8-Å crystal structure of the intact maltose transporter in complex with the maltose-binding protein, maltose and ATP provides direct evidence for a concerted mechanism of transport in which solute is transferred from the binding protein to the transmembrane subunits when the cassette dimer closes to hydrolyse ATP.
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Mechanism of maltose transport in Escherichia coli: transmembrane signaling by periplasmic binding proteins.
TL;DR: The results suggest that ATP hydrolysis is not directly coupled to ligand transport even in wild-type cells and that one important function of MBP is to transmit a transmembrane signal, through the membrane-spanning MalF and MalG proteins, to the MalK protein on the other side of the membrane, so that ATP Hydrolysis can occur.