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| Chinese scholars have resolved the tubular transport channel protein of mycobacteria |
The reporter learned from the University of Science and Technology of China on the 4th that Professor Gong Weimin from the National Research Center for Microscale Material Science of the university and collaborators have determined the unknown functional protein Rv3705c and Rv3705c in Mycobacterium tuberculosis through X-ray crystallography and cryo-electron microscopy.
The three-dimensional structure of its homologous protein MSMEG_6251 in Mycobacterium smegmatis was found to be able to self-assemble into a tubular structure in vitro
.
Through a series of molecular biology and biochemical experiments, it was shown that the protein played a channel role on the outer membrane of mycobacteria, and the protein was named TiME
Mycobacteria have a very complex envelope structure, including the plasma membrane, cell wall and capsule from the inside to the outside
.
Among them, the cell wall is composed of three covalently connected layers, from the inside to the outside in sequence: a peptidoglycan layer, an arabinogalactan layer, and a mycobacteric acid layer surrounded by glycolipids non-covalently
Researchers have discovered through research that TiME forms a ring structure with an inner diameter of nearly 60 angstroms in an eightfold symmetrical manner.
Two single-layer rings form a double-layer ring in a tail-to-tail manner, and the double-layer ring is repeatedly stacked as the basic unit.
It is a tubular structure
.
Cell localization experiments of Mycobacterium smegmatis confirmed that TiME protein is mainly distributed in the envelope, especially in the outer membrane and capsule
This research result was the first to discover material transport channels in mycobacterial capsules, providing new clues and ideas for studying the material transport mechanism of pathogenic mycobacteria and developing new drug targets
