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PDBsum entry 3dkt
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Structural protein/virus like particle
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PDB id
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3dkt
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References listed in PDB file
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Key reference
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Title
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Structural basis of enzyme encapsulation into a bacterial nanocompartment.
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Authors
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M.Sutter,
D.Boehringer,
S.Gutmann,
S.Günther,
D.Prangishvili,
M.J.Loessner,
K.O.Stetter,
E.Weber-Ban,
N.Ban.
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Ref.
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Nat Struct Biol, 2008,
15,
939-947.
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PubMed id
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Abstract
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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.
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