3DKT
Crystal structure of Thermotoga maritima encapsulin
Summary for 3DKT
| Entry DOI | 10.2210/pdb3dkt/pdb |
| Descriptor | Maritimacin, Putative uncharacterized protein (3 entities in total) |
| Functional Keywords | enzyme encapsulation, nanocompartment, oxidative stress, ferritin-like protein, hk97-fold, antibiotic, antimicrobial, bacteriocin, cobalt, hydrolase, protease, secreted, structural protein-virus like particle complex, structural protein/virus like particle |
| Biological source | Thermotoga maritima More |
| Total number of polymer chains | 20 |
| Total formula weight | 313337.35 |
| Authors | Sutter, M.,Boehringer, D.,Gutmann, S.,Weber-Ban, E.,Ban, N. (deposition date: 2008-06-26, release date: 2008-09-02, Last modification date: 2024-03-20) |
| Primary citation | Sutter, M.,Boehringer, D.,Gutmann, S.,Gunther, S.,Prangishvili, D.,Loessner, M.J.,Stetter, K.O.,Weber-Ban, E.,Ban, N. Structural basis of enzyme encapsulation into a bacterial nanocompartment Nat.Struct.Mol.Biol., 15:939-947, 2008 Cited by PubMed Abstract: Compartmentalization is an important organizational feature of life. It occurs at varying levels of complexity ranging from eukaryotic organelles and the bacterial microcompartments, to the molecular reaction chambers formed by enzyme assemblies. The structural basis of enzyme encapsulation in molecular compartments is poorly understood. Here we show, using X-ray crystallographic, biochemical and EM experiments, that a widespread family of conserved bacterial proteins, the linocin-like proteins, form large assemblies that function as a minimal compartment to package enzymes. We refer to this shell-forming protein as 'encapsulin'. The crystal structure of such a particle from Thermotoga maritima determined at 3.1-angstroms resolution reveals that 60 copies of the monomer assemble into a thin, icosahedral shell with a diameter of 240 angstroms. The interior of this nanocompartment is lined with conserved binding sites for short polypeptide tags present as C-terminal extensions of enzymes involved in oxidative-stress response. PubMed: 19172747DOI: 10.1038/nsmb.1473 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.104 Å) |
Structure validation
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