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TitleStructural basis of enzyme encapsulation into a bacterial nanocompartment.
Journal, issue, pagesNat Struct Mol Biol, Vol. 15, Issue 9, Page 939-947, Year 2008
Publish dateFeb 19, 2009
AuthorsMarkus Sutter / Daniel Boehringer / Sascha Gutmann / Susanne Günther / David Prangishvili / Martin J Loessner / Karl O Stetter / Eilika Weber-Ban / Nenad Ban /
PubMed AbstractCompartmentalization 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 ...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.
External linksNat Struct Mol Biol / PubMed:19172747
MethodsEM (single particle) / X-ray diffraction
Resolution3.104 - 16.0 Å
Structure data

EMDB-1530:
Structure of hexameric DyP from Brevibacterium linens
Method: EM (single particle) / Resolution: 16.0 Å

PDB-3dkt:
Crystal structure of Thermotoga maritima encapsulin
Method: X-RAY DIFFRACTION / Resolution: 3.104 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • Brevibacterium linens (bacteria)
  • thermotoga maritima (bacteria)
KeywordsSTRUCTURAL PROTEIN/VIRUS LIKE PARTICLE / enzyme encapsulation / nanocompartment / oxidative stress / ferritin-like protein / hk97-fold / Antibiotic / Antimicrobial / Bacteriocin / Cobalt / Hydrolase / Protease / Secreted / STRUCTURAL PROTEIN-VIRUS LIKE PARTICLE COMPLEX

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