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PDBsum entry 3dkt

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protein ligands Protein-protein interface(s) links
Structural protein/virus like particle PDB id
3dkt
Jmol
Contents
Protein chains
(+ 4 more) 264 a.a. *
Ligands
GLY-GLY-ASP-LEU-
GLY-ILE-ARG-LYS
×10
Waters ×100
* Residue conservation analysis
PDB id:
3dkt
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
Resolution:
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
Date:
26-Jun-08     Release date:   02-Sep-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9WZP2  (MARIT_THEMA) -  Maritimacin
Seq:
Struc:
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.
 
  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 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.  
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.