5ZUL

Small heat shock protein from Mycobacterium marinum M : Form-3

5ZUL の概要

• エントリーDOI: 10.2210/pdb5zul/pdb
• 分子名称: Small heat shock protein (1 entity in total)
• 機能のキーワード: shsp, oligomers, polydispersity, chaperone
• 由来する生物種: Mycobacterium marinum M
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 99214.82

構造登録者

Bhandari, S.,Suguna, K. (登録日: 2018-05-08, 公開日: 2019-01-30, 最終更新日: 2023-11-22)

主引用文献

Bhandari, S.,Biswas, S.,Chaudhary, A.,Dutta, S.,Suguna, K.
Dodecameric structure of a small heat shock protein from Mycobacterium marinum M.
Proteins, 87:365-379, 2019

PubMed Abstract: Small heat shock proteins (sHSPs) are ATP-independent molecular chaperones present ubiquitously in all kingdoms of life. Their low molecular weight subunits associate to form higher order structures. Under conditions of stress, sHSPs prevent aggregation of substrate proteins by undergoing rapid changes in their conformation or stoichiometry. Polydispersity and dynamic nature of these proteins have made structural investigations through crystallography a daunting task. In pathogens like Mycobacteria, sHSPs are immuno-dominant antigens, enabling survival of the pathogen within the host and contributing to disease persistence. We characterized sHSPs from Mycobacterium marinum M and determined the crystal structure of one of these. The protein crystallized in three different conditions as dodecamers, with dimers arranged in a tetrahedral fashion to form a closed cage-like architecture. Interestingly, we found a pentapeptide bound to the dodecamers revealing one of the modes of sHSP-substrate interaction. Further, we have observed that ATP inhibits the chaperoning activity of the protein.

PubMed: 30632633
DOI: 10.1002/prot.25657

実験手法

X-RAY DIFFRACTION (3.75 Å)