1SJP

Mycobacterium tuberculosis Chaperonin60.2

1SJP の概要

• エントリーDOI: 10.2210/pdb1sjp/pdb
• 分子名称: 60 kDa chaperonin 2 (1 entity in total)
• 機能のキーワード: chaperone, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc
• 由来する生物種: Mycobacterium tuberculosis
• 細胞内の位置: Cytoplasm (By similarity): P0A520
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 106097.98

構造登録者

Qamra, R.,Mande, S.C.,TB Structural Genomics Consortium (TBSGC) (登録日: 2004-03-04, 公開日: 2004-12-07, 最終更新日: 2023-10-25)

主引用文献

Qamra, R.,Mande, S.C.
Crystal Structure of the 65-Kilodalton Heat Shock Protein, Chaperonin 60.2, of Mycobacterium tuberculosis
J.Bacteriol., 186:8105-8113, 2004

PubMed Abstract: Chaperonin 60s are a ubiquitous class of proteins that promote folding and assembly of other cellular polypeptides in an ATP-dependent manner. The oligomeric state of chaperonin 60s has been shown to be crucial to their role as molecular chaperones. Chaperonin 60s are also known to be important stimulators of the immune system. Mycobacterium tuberculosis possesses a duplicate set of chaperonin 60s, both of which have been shown to be potent cytokine stimulators. The M. tuberculosis chaperonin 60s are present in the extracellular milieu at concentrations that are extremely low for the formation of an oligomer. Here we present the crystal structure of one of the chaperonin 60s of M. tuberculosis, also called Hsp65 or chaperonin 60.2, at 3.2-A resolution. We were able to crystallize the protein in its dimeric state. The unusual dimerization of the protein leads to exposure of certain hydrophobic patches on the surface of the protein, and we hypothesize that this might have relevance in binding to immunogenic peptides, as it does in the eukaryotic homologs.

PubMed: 15547284
DOI: 10.1128/JB.186.23.8105-8113.2004

実験手法

X-RAY DIFFRACTION (3.2 Å)