3M6C

Crystal structure of Mycobacterium tuberculosis GroEL1 apical domain

3M6C の概要

• エントリーDOI: 10.2210/pdb3m6c/pdb
• 分子名称: 60 kDa chaperonin 1 (2 entities in total)
• 機能のキーワード: chaperone, atp-binding, nucleotide-binding
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20746.69

構造登録者

Tsai, F.T.F.,Sielaff, B.,Lee, K. (登録日: 2010-03-15, 公開日: 2010-12-08, 最終更新日: 2023-09-06)

主引用文献

Sielaff, B.,Lee, K.S.,Tsai, F.T.
Structural and functional conservation of Mycobacterium tuberculosis GroEL paralogs suggests that GroEL1 Is a chaperonin.
J.Mol.Biol., 405:831-839, 2011

PubMed Abstract: GroEL is a group I chaperonin that facilitates protein folding and prevents protein aggregation in the bacterial cytosol. Mycobacteria are unusual in encoding two or more copies of GroEL in their genome. While GroEL2 is essential for viability and likely functions as the general housekeeping chaperonin, GroEL1 is dispensable, but its structure and function remain unclear. Here, we present the 2.2-Å resolution crystal structure of a 23-kDa fragment of Mycobacterium tuberculosis GroEL1 consisting of an extended apical domain. Our X-ray structure of the GroEL1 apical domain closely resembles those of Escherichia coli GroEL and M. tuberculosis GroEL2, thus highlighting the remarkable structural conservation of bacterial chaperonins. Notably, in our structure, the proposed substrate-binding site of GroEL1 interacts with the N-terminal region of a symmetry-related neighboring GroEL1 molecule. The latter is consistent with the known GroEL apical domain function in substrate binding and is supported by results obtained from using peptide array technology. Taken together, these data show that the apical domains of M. tuberculosis GroEL paralogs are conserved in three-dimensional structure, suggesting that GroEL1, like GroEL2, is a chaperonin.

PubMed: 21094166
DOI: 10.1016/j.jmb.2010.11.021

実験手法

X-RAY DIFFRACTION (2.2 Å)