This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.The maltose transport complex of Escherichia coli, a member of the ATP-binding cassette (ABC) superfamily, mediates the high affinity uptake maltose at the expense of ATP. The membrane-associated transporter consists of two transmembrane subunits, MalF and MalG and two copies of the cytoplasmic ATP-binding cassette subunit, MalK. The structure for MalK2 at ATP-bound and ATP-free forms have been determined by X-ray crystallography, but the structure of MalF, MalG and MalFGK2 still remains unknown. Cryo-EM and single particle image analysis of MalFGK2 is the aim of this project.
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