7K3Z

P. falciparum Cpn60 D474A mutant bound to ATP

Summary for 7K3Z

• Entry DOI: 10.2210/pdb7k3z/pdb
• Descriptor: 60 kDa chaperonin, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• Functional Keywords: malaria, mitochondrial protein, chaperone
• Biological source: Plasmodium falciparum (isolate 3D7)
• Total number of polymer chains: 7
• Total formula weight: 446654.26

Authors

Tolia, N.H.,Shi, D.,Nguyen, B. (deposition date: 2020-09-14, release date: 2021-04-21, Last modification date: 2023-10-18)

Primary citation

Nguyen, B.,Ma, R.,Tang, W.K.,Shi, D.,Tolia, N.H.
Crystal structure of P. falciparum Cpn60 bound to ATP reveals an open dynamic conformation before substrate binding.
Sci Rep, 11:5930-5930, 2021

PubMed Abstract: Plasmodium falciparum harbors group 1 and group 2 chaperonin systems to mediate the folding of cellular proteins in different cellular locations. Two distinct group 1 chaperonins operate in the organelles of mitochondria and apicoplasts, while group 2 chaperonins function in the cytosol. No structural information has been reported for any chaperonin from plasmodium. In this study, we describe the crystal structure of a double heptameric ring Plasmodium falciparum mitochondrial chaperonin 60 (Cpn60) bound with ATP, which differs significantly from any known crystal structure of chaperonin 60. The structure likely represents a unique intermediate state during conformational conversion from the closed state to the opened state. Three of the seven apical domains are highly dynamic while the equatorial domains form a stable ring. The structure implies large movements of the apical domain in the solution play a role in nucleotide-dependent regulation of substrate binding and folding. A unique 26-27 residue insertion in the equatorial domain of Plasmodium falciparum mitochondrial chaperonin greatly increases both inter-ring and intra-ring subunit-subunit interactions. The present structure provides new insights into the mechanism of Cpn60 in chaperonin assembly and function.

PubMed: 33723304
DOI: 10.1038/s41598-021-85197-3

Experimental method

X-RAY DIFFRACTION (3.69 Å)