Cryo-EM structure of ATPγS-DppBCDF.

<p>(<b>A</b>) Cartoon representation of the ATPγS-DppBCDF structure. Color scheme same as in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003026#pbio.3003026.g001" target="_blank">Fig 1</a>. The EM density of ATPγS in Dp...

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Bibliographic Details
Main Author:	Panpan Li (484033) (author)
Other Authors:	Manfeng Zhang (8996972) (author), Yihua Huang (245089) (author)
Published:	2025
Subjects:	Biophysics Biochemistry Microbiology Cell Biology Molecular Biology Biotechnology Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified various physiological processes five distinct subunits div >< p avoiding dipeptides escaping bound dppabcdf adopts preventing dipeptide back mycobacterium tuberculosis </ dipeptide transporter dppabcdf structural studies reveal escherichia coli </ abc transporter dppabcdf bound dppbcdf adopts amppnp molecule bound coli </ complexes bound dipeptide acquisition structural observations structural characterization reveals insights reported heterotrimeric periplasm upon peptide transporters negative bacteria intracellular targets important role forth binding facing conformation em structures dppbcdf translocator dppbcd translocator binding cassette atpase subunit
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Cryo-EM structure of ATPγS-DppBCDF.

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