4pj1
Crystal structure of the human mitochondrial chaperonin symmetrical 'football' complexCrystal structure of the human mitochondrial chaperonin symmetrical 'football' complex
Structural highlights
Disease[CH60_HUMAN] Autosomal dominant spastic paraplegia type 13;Pelizaeus-Merzbacher-like disease due to HSPD1 mutation. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. Function[CH60_HUMAN] Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. [CH10_HUMAN] Eukaryotic CPN10 homolog which is essential for mitochondrial protein biogenesis, together with CPN60. Binds to CPN60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. Publication Abstract from PubMedThe 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. Crystallization and structure determination of a symmetrical 'football' complex of the mammalian mitochondrial Hsp60-Hsp10 chaperonins.,Nisemblat S, Parnas A, Yaniv O, Azem A, Frolow F Acta Crystallogr F Struct Biol Commun. 2014 Jan;70(Pt 1):116-9. doi:, 10.1107/S2053230X1303389X. Epub 2013 Dec 24. PMID:24419632[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||