7AZP

Structure of the human mitochondrial HSPD1 single ring

Summary for 7AZP

• Entry DOI: 10.2210/pdb7azp/pdb
• EMDB information: 11189 11950
• Descriptor: 60 kDa heat shock protein, mitochondrial (1 entity in total)
• Functional Keywords: hspd1, hsp60, chaperonin, chaperone
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 7
• Total formula weight: 408148.84

Authors

Klebl, D.P.,Feasey, M.C.,Muench, S.P. (deposition date: 2020-11-17, release date: 2021-02-10, Last modification date: 2024-05-01)

Primary citation

Klebl, D.P.,Feasey, M.C.,Hesketh, E.L.,Ranson, N.A.,Wurdak, H.,Sobott, F.,Bon, R.S.,Muench, S.P.
Cryo-EM structure of human mitochondrial HSPD1.
Iscience, 24:102022-102022, 2021

PubMed Abstract: Chaperonins play an important role in folding newly synthesized or translocated proteins in all organisms. The bacterial chaperonin GroEL has served as a model system for the understanding of these proteins. In comparison, its human homolog, known as mitochondrial heat shock protein family member D1 (HSPD1) is poorly understood. Here, we present the structure of HSPD1 in the apo state determined by cryo-electron microscopy (cryo-EM). Unlike GroEL, HSPD1 forms mostly single ring assemblies in the absence of co-chaperonin (HSPE1). Comparison with GroEL shows a rotation and increased flexibility of the apical domain. Together with published structures of the HSPD1/HSPE1 co-chaperonin complex, this work gives insight into the structural changes that occur during the catalytic cycle. This new understanding of HSPD1 structure and its rearrangements upon complex formation may provide new insights for the development of HSPD1-targeting treatments against a diverse range of diseases including glioblastoma.

PubMed: 33506187
DOI: 10.1016/j.isci.2020.102022

Experimental method

ELECTRON MICROSCOPY (3.5 Å)