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Literature summary extracted from

  • Qamra, R.; Mande, S.C.
    Crystal structure of the 65-kilodalton heat shock protein, chaperonin 60.2, of Mycobacterium tuberculosis (2004), J. Bacteriol., 186, 8105-8113.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.6.1.7 expression in Escherichia coli Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.6.1.7 hanging drop vapor diffusion method by using a reservoir solution containing 100 mM HEPES (pH 7.5), 25% (wt/vol) polyethylene glycol 3350, and 10% (vol/vol) n-propanol, 3.2 A resolution Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
5.6.1.7 Mycobacterium tuberculosis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.6.1.7
-
 Mycobacterium tuberculosis

Subunits

EC Number Subunits Comment Organism
5.6.1.7 dimer the unusual dimerization of the protein leads to exposure of certain hydrophobic patches on the surface of the protein, and it is hypothesized that this might have relevance in binding to immunogenic peptides, as it does in the eukaryotic homologs Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
5.6.1.7 chaperonin 60.2
-
 Mycobacterium tuberculosis
5.6.1.7 heat shock protein chaperonin 60.2
-
 Mycobacterium tuberculosis
5.6.1.7 Hsp65
-
 Mycobacterium tuberculosis