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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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Contents |
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* Residue conservation analysis
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PDB id:
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Structural protein/virus like particle
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Title:
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Crystal structure of thermotoga maritima encapsulin
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Structure:
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Maritimacin. Chain: a, b, c, d, e, f, g, h, i, j. Synonym: thermotoga bacteriocin. Putative uncharacterized protein. Chain: k, l, m, n, o, p, q, r, s, t. Fragment: c-terminal encapsulin binding peptide, unp residues 106- 113'. Synonym: ferritin-like protein
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Source:
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Thermotoga maritima. Organism_taxid: 2336. Strain: msb8, dsm3109. Strain: msb8, dsm3109
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Resolution:
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3.10Å
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R-factor:
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0.220
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R-free:
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0.239
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Authors:
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M.Sutter,D.Boehringer,S.Gutmann,E.Weber-Ban,N.Ban
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Key ref:
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M.Sutter
et al.
(2008).
Structural basis of enzyme encapsulation into a bacterial nanocompartment.
Nat Struct Biol,
15,
939-947.
PubMed id:
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Date:
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26-Jun-08
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Release date:
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02-Sep-08
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PROCHECK
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Headers
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References
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Q9WZP2
(MARIT_THEMA) -
Type 1 encapsulin shell protein from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
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Seq:
Struc:
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265 a.a.
264 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Nat Struct Biol
15:939-947
(2008)
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PubMed id:
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Structural basis of enzyme encapsulation into a bacterial nanocompartment.
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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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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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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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S.Kang,
and
T.Douglas
(2010).
Biochemistry. Some enzymes just need a space of their own.
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Science,
327,
42-43.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
