PDBsum entry 3dkt

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Structural protein/virus like particle PDB id
Protein chains
(+ 4 more) 264 a.a. *
Waters ×100
* Residue conservation analysis
PDB id:
Name: Structural protein/virus like particle
Title: Crystal structure of thermotoga maritima encapsulin
Structure: 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 residu 113'. Synonym: ferritin-like protein
Source: Thermotoga maritima. Organism_taxid: 2336. Strain: msb8, dsm3109. Strain: msb8, dsm3109
3.10Å     R-factor:   0.220     R-free:   0.239
Authors: M.Sutter,D.Boehringer,S.Gutmann,E.Weber-Ban,N.Ban
Key ref: M.Sutter et al. (2008). Structural basis of enzyme encapsulation into a bacterial nanocompartment. Nat Struct Mol Biol, 15, 939-947. PubMed id: 19172747
26-Jun-08     Release date:   02-Sep-08    
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Protein chains
Pfam   ArchSchema ?
Q9WZP2  (MARIT_THEMA) -  Maritimacin
265 a.a.
264 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biological process     cytolysis   3 terms 
  Biochemical function     hydrolase activity     2 terms  


Nat Struct Mol Biol 15:939-947 (2008)
PubMed id: 19172747  
Structural basis of enzyme encapsulation into a bacterial nanocompartment.
M.Sutter, D.Boehringer, S.Gutmann, S.Günther, D.Prangishvili, M.J.Loessner, K.O.Stetter, E.Weber-Ban, N.Ban.
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.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20044564 S.Kang, and T.Douglas (2010).
Biochemistry. Some enzymes just need a space of their own.
  Science, 327, 42-43.  
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