Recombinant Chlamydia trachomatis Chaperonin GroEL (groEL)

The expression region of this recombinant Chlamydia trachomatis (strain D/UW-3/Cx) groL covers amino acids 2-544. The calculated molecular weight for this groL protein is 74.0 kDa. Expression of this groL protein is conducted in e.coli. The N-terminal 6xHis-SUMO tag was smoothly integrated into the coding gene of groL, which enables a simple process of detecting and purifying the groL recombinant protein in the following steps.

The Chaperonin GroEL is a protein encoded by the groEL gene in Chlamydia trachomatis. Chaperonins are molecular chaperones that assist in the proper folding of newly synthesized or stress-denatured proteins. GroEL forms a complex with its co-chaperonin GroES, creating a barrel-like structure that provides a confined environment for the folding of substrate proteins. The Chlamydia trachomatis Chaperonin GroEL likely plays a crucial role in the correct folding of proteins within the bacterium, ensuring their functional integrity. Proper protein folding is essential for various cellular processes, including virulence and survival within the host. Understanding the function of Chaperonin GroEL in Chlamydia trachomatis can provide insights into the pathogenic mechanisms of this obligate intracellular bacterium and may contribute to the development of therapeutic strategies.