4PJ1

Crystal structure of the human mitochondrial chaperonin symmetrical 'football' complex

Summary for 4PJ1

• Entry DOI: 10.2210/pdb4pj1/pdb
• Descriptor: 60 kDa heat shock protein, mitochondrial, 10 kDa heat shock protein, mitochondrial, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: human, mitochondrial, chaperonin, complex, symmetric, chaperone
• Biological source: Homo sapiens (Human); More
• Cellular location: Mitochondrion matrix: P10809 P61604
• Total number of polymer chains: 28
• Total formula weight: 1017047.09

Authors

Frolow, F.,Azem, A.,Nisemblat, S. (deposition date: 2014-05-10, release date: 2015-04-29, Last modification date: 2023-09-27)

Primary citation

Nisemblat, S.,Yaniv, O.,Parnas, A.,Frolow, F.,Azem, A.
Crystal structure of the human mitochondrial chaperonin symmetrical football complex.
Proc.Natl.Acad.Sci.USA, 112:6044-6049, 2015

PubMed Abstract: Human mitochondria harbor a single type I chaperonin system that is generally thought to function via a unique single-ring intermediate. To date, no crystal structure has been published for any mammalian type I chaperonin complex. In this study, we describe the crystal structure of a football-shaped, double-ring human mitochondrial chaperonin complex at 3.15 Å, which is a novel intermediate, likely representing the complex in an early stage of dissociation. Interestingly, the mitochondrial chaperonin was captured in a state that exhibits subunit asymmetry within the rings and nucleotide symmetry between the rings. Moreover, the chaperonin tetradecamers show a different interring subunit arrangement when compared to GroEL. Our findings suggest that the mitochondrial chaperonins use a mechanism that is distinct from the mechanism of the well-studied Escherichia coli system.

PubMed: 25918392
DOI: 10.1073/pnas.1411718112

Experimental method

X-RAY DIFFRACTION (3.15 Å)