Crystallization and structure determination of a symmetrical 'football' complex of the mammalian mitochondrial Hsp60-Hsp10 chaperonins

Shahar Nisemblat, Avital Parnas, Oren Yaniv, Abdussalam Azem*, Felix Frolow

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

24 Scopus citations

Abstract

The mitochondrial Hsp60-Hsp10 complex assists the folding of various proteins impelled by ATP hydrolysis, similar to the bacterial chaperonins GroEL and GroES. The near-Atomic structural details of the mitochondrial chaperonins are not known, despite the fact that almost two decades have passed since the structures of the bacterial chaperonins became available. Here, the crystallization procedure, diffraction experiments and structure determination by molecular replacement of the mammalian mitochondrial chaperonin HSP60 (E321K mutant) and its co-chaperonin Hsp10 are reported.

Original languageEnglish
Pages (from-to)116-119
Number of pages4
JournalActa Crystallographica Section F:Structural Biology Communications
Volume70
Issue number1
DOIs
StatePublished - Jan 2014

Keywords

  • mHsp10
  • mHsp60
  • mitochondrial chaperonins

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