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Negative Stain Single-particle EM of the Maltose Transporter in Nanodiscs Reveals Asymmetric Closure of MalK₂ and Catalytic Roles of ATP, MalE, and Maltose.

ABSTRACT: The Escherichia coli MalE-MalFGK₂ complex is one of the best characterized members of the large and ubiquitous family of ATP-binding cassette (ABC) transporters. It is composed of a membrane-spanning heterodimer, MalF-MalG; a homodimeric ATPase, MalK₂; and a periplasmic maltose receptor, MalE. Opening and closure of MalK₂ is coupled to conformational changes in MalF-MalG and the alternate exposition of the substrate-binding site to either side of the membrane. To further define this alternate access mechanism and the impact of ATP, MalE, and maltose on the conformation of the transporter during the transport cycle, we have reconstituted MalFGK₂ in nanodiscs and analyzed its conformations under 10 different biochemical conditions using nega

SUBMITTER: Fabre L

PROVIDER: S-EPMC5392688 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature

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Negative Stain Single-particle EM of the Maltose Transporter in Nanodiscs Reveals Asymmetric Closure of MalK₂ and Catalytic Roles of ATP, MalE, and Maltose.

OmicsDI is part of the ELIXIR infrastructure

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Dataset Information

Negative Stain Single-particle EM of the Maltose Transporter in Nanodiscs Reveals Asymmetric Closure of MalK2 and Catalytic Roles of ATP, MalE, and Maltose.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Negative Stain Single-particle EM of the Maltose Transporter in Nanodiscs Reveals Asymmetric Closure of MalK₂ and Catalytic Roles of ATP, MalE, and Maltose.