Literature summary for 5.6.1.7 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.

Search for more literature for 5.6.1.7

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Mycobacterium tuberculosis

Subunits

Subunits	Comment	Organism
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

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

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Release 2023.1 (January 2023)