5UYZ

Structure of Human T-complex protein 1 subunit epsilon (CCT5) mutant His147Arg

Summary for 5UYZ

• Entry DOI: 10.2210/pdb5uyz/pdb
• Related: 5uyx
• Descriptor: T-complex protein 1 subunit epsilon, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION (3 entities in total)
• Functional Keywords: chaperonin hexadecameric complex atp-dependent cct5 gene, protein binding
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm : P48643
• Total number of polymer chains: 4
• Total formula weight: 240857.74

Authors

Pereira, J.H.,McAndrew, R.P.,Sergeeva, O.A.,Ralston, C.Y.,King, J.A.,Adams, P.D. (deposition date: 2017-02-24, release date: 2017-07-05, Last modification date: 2023-10-04)

Primary citation

Pereira, J.H.,McAndrew, R.P.,Sergeeva, O.A.,Ralston, C.Y.,King, J.A.,Adams, P.D.
Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy.
Sci Rep, 7:3673-3673, 2017

PubMed Abstract: The human chaperonin TRiC consists of eight non-identical subunits, and its protein-folding activity is critical for cellular health. Misfolded proteins are associated with many human diseases, such as amyloid diseases, cancer, and neuropathies, making TRiC a potential therapeutic target. A detailed structural understanding of its ATP-dependent folding mechanism and substrate recognition is therefore of great importance. Of particular health-related interest is the mutation Histidine 147 to Arginine (H147R) in human TRiC subunit 5 (CCT5), which has been associated with hereditary sensory neuropathy. In this paper, we describe the crystal structures of CCT5 and the CCT5-H147R mutant, which provide important structural information for this vital protein-folding machine in humans. This first X-ray crystallographic study of a single human CCT subunit in the context of a hexadecameric complex can be expanded in the future to the other 7 subunits that form the TRiC complex.

PubMed: 28623285
DOI: 10.1038/s41598-017-03825-3

Experimental method

X-RAY DIFFRACTION (3.6 Å)