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TitleCryo-EM structure of human mitochondrial HSPD1.
Journal, issue, pagesiScience, Vol. 24, Issue 1, Page 102022, Year 2021
Publish dateJan 22, 2021
AuthorsDavid P Klebl / Matthew C Feasey / Emma L Hesketh / Neil A Ranson / Heiko Wurdak / Frank Sobott / Robin S Bon / Stephen P Muench /
PubMed AbstractChaperonins 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 ...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.
External linksiScience / PubMed:33506187 / PubMed Central
MethodsEM (single particle)
Resolution3.5 - 4.9 Å
Structure data

EMDB-11189:
Structure of human mitochondrial HSPD1 as an inverted double ring
Method: EM (single particle) / Resolution: 4.9 Å

11950

7azp

EMDB-11950, PDB-7azp:
Structure of the human mitochondrial HSPD1 single ring
Method: EM (single particle) / Resolution: 3.5 Å

Source
  • homo sapiens (human)
KeywordsCHAPERONE / HSPD1 / Hsp60 / chaperonin

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