encapsulin nanocompartment / Hydrolases; Acting on peptide bonds (peptidases) / peptidase activity / iron ion transport / intracellular iron ion homeostasis / proteolysis Similarity search - Function
Major capsid protein gp5 fold - #30 / hypothetical protein PF0899 domain / Major capsid protein gp5 fold / Ferritin-like protein / hypothetical protein PF0899 fold / : / Type 1 encapsulin shell protein / Encapsulating protein for peroxidase / Ferritin-like / Ferritin-like superfamily ...Major capsid protein gp5 fold - #30 / hypothetical protein PF0899 domain / Major capsid protein gp5 fold / Ferritin-like protein / hypothetical protein PF0899 fold / : / Type 1 encapsulin shell protein / Encapsulating protein for peroxidase / Ferritin-like / Ferritin-like superfamily / 2-Layer Sandwich / Alpha Beta Similarity search - Domain/homology
Journal: Nat Struct Mol Biol / Year: 2008 Title: Structural basis of enzyme encapsulation into a bacterial nanocompartment. Authors: Markus Sutter / Daniel Boehringer / Sascha Gutmann / Susanne Günther / David Prangishvili / Martin J Loessner / Karl O Stetter / Eilika Weber-Ban / Nenad Ban / 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 ...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.
History
Deposition
Jun 26, 2008
Deposition site: RCSB / Processing site: PDBJ
Revision 1.0
Sep 2, 2008
Provider: repository / Type: Initial release
Revision 1.1
Jul 13, 2011
Group: Version format compliance
Revision 1.2
Aug 24, 2011
Group: Database references
Revision 1.3
Aug 31, 2011
Group: Database references / Source and taxonomy
Revision 1.4
Nov 6, 2019
Group: Data collection / Category: reflns_shell / Item: _reflns_shell.Rmerge_I_obs
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