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Title: Discuss the structure of the chaperonin GroESGroEL complex found in E. coli. What will be an ... Post by: ugai_kyut on Feb 4, 2018 Discuss the structure of the chaperonin GroESGroEL complex found in E. coli.
What will be an ideal response? Title: Discuss the structure of the chaperonin GroESGroEL complex found in E. coli. What will be an ... Post by: jogden1011 on Feb 4, 2018 ANSWER: In the GroESGroEL complex, GroEL is a protein made of two stacked seven-membered rings of 60-kD subunits that form a cylindrical 14 oligomer 15 nm high and 14 nm wide. Each GroEL ring has a 5-nm central cavity where folding can take place. This cavity can accommodate proteins up to 60 kD in size. GroES, sometimes referred to as a co-chaperonin, consists of a single seven-membered ring of 10-kD subunits that sits like a dome on one end of GroEL. The end of GroEL where GroES is sitting is referred to as the apical end. Each GroEL subunit has two structural domains: an equatorial domain that binds ATP and interacts with neighbors in the other 7 ring and an apical domain with hydrophobic residues that can interact with hydrophobic regions on partially folded proteins.
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