Structural and functional conservation of Mycobacterium tuberculosis GroEL paralogs suggests that GroEL1 Is a chaperonin.
Structural and functional conservation of Mycobacterium tuberculosis GroEL paralogs suggests that GroEL1 Is a chaperonin.
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DOI:
10.1016/j.jmb.2010.11.021
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发表时间:
2011-01-21
影响因子:
5.6
通讯作者:
Tsai FT
中科院分区:
文献类型:
--
作者:
Sielaff B;Lee KS;Tsai FT
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, we show that the apical domains of M. tuberculosis GroEL paralogs are conserved in three-dimensional structure, suggesting that GroEL1, like GroEL2, is a chaperonin.
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