2BYU
Negative stain EM reconstruction of M.tuberculosis Acr1(Hsp 16.3) fitted with wheat sHSP dimer
Summary for 2BYU
| Entry DOI | 10.2210/pdb2byu/pdb |
| Related | 1GME |
| EMDB information | 1149 |
| Descriptor | HEAT SHOCK PROTEIN 16.9B (1 entity in total) |
| Functional Keywords | small heat shock protein, alpha-crystallin, chaperone |
| Biological source | TRITICUM AESTIVUM (WHEAT) |
| Total number of polymer chains | 12 |
| Total formula weight | 148513.79 |
| Authors | Kennaway, C.K.,Benesch, J.L.P.,Gohlke, U.,Wang, L.,Robinson, C.V.,Orlova, E.V.,Saibil, H.R.,Keep, N.H. (deposition date: 2005-08-05, release date: 2005-08-22, Last modification date: 2024-05-08) |
| Primary citation | 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 Cited by 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: 16046399DOI: 10.1074/JBC.M504263200 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (16.5 Å) |
Structure validation
Download full validation report
