2BYU

Negative stain EM reconstruction of M.tuberculosis Acr1(Hsp 16.3) fitted with wheat sHSP dimer

2BYU の概要

• エントリーDOI: 10.2210/pdb2byu/pdb
• 関連するPDBエントリー: 1GME
• EMDBエントリー: 1149
• 分子名称: HEAT SHOCK PROTEIN 16.9B (1 entity in total)
• 機能のキーワード: small heat shock protein, alpha-crystallin, chaperone
• 由来する生物種: TRITICUM AESTIVUM (WHEAT)
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 148513.79

構造登録者

Kennaway, C.K.,Benesch, J.L.P.,Gohlke, U.,Wang, L.,Robinson, C.V.,Orlova, E.V.,Saibil, H.R.,Keep, N.H. (登録日: 2005-08-05, 公開日: 2005-08-22, 最終更新日: 2024-05-08)

主引用文献

Kennaway, C.K.,Benesch, J.L.P.,Gohlke, U.,Wang, L.,Robinson, C.V.,Orlova, E.V.,Saibil, H.R.,Keep, N.H.
Dodecameric Structure of the Small Heat Shock Protein Acr1 from Mycobacterium Tuberculosis.
J.Biol.Chem., 280:33419-, 2005

PubMed Abstract: Small heat shock proteins are a ubiquitous and diverse family of stress proteins that have in common an alpha-crystallin domain. Mycobacterium tuberculosis has two small heat shock proteins, Acr1 (alpha-crystallin-related protein 1, or Hsp16.3/16-kDa antigen) and Acr2 (HrpA), both of which are highly expressed under different stress conditions. Small heat shock proteins form large oligomeric assemblies and are commonly polydisperse. Nanoelectrospray mass spectrometry showed that Acr2 formed a range of oligomers composed of dimers and tetramers, whereas Acr1 was a dodecamer. Electron microscopy of Acr2 showed a variety of particle sizes. Using three-dimensional analysis of negative stain electron microscope images, we have shown that Acr1 forms a tetrahedral assembly with 12 polypeptide chains. The atomic structure of a related alpha-crystallin domain dimer was docked into the density to build a molecular structure of the dodecameric Acr1 complex. Along with the differential regulation of these two proteins, the differences in their quaternary structures demonstrated here supports their distinct functional roles.

PubMed: 16046399
DOI: 10.1074/JBC.M504263200

実験手法

ELECTRON MICROSCOPY (16.5 Å)