4pj1

From Proteopedia

(Difference between revisions)

Revision as of 06:30, 13 May 2015

Crystal structure of the human mitochondrial chaperonin symmetrical 'football' complex

Structural highlights

4pj1 is a 28 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, RCSB, PDBsum

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 PubMed

Human mitochondria harbor a single type I chaperonin system that is generally thought to function via a unique single-ring intermediate. To date, no crystal structure has been published for any mammalian type I chaperonin complex. In this study, we describe the crystal structure of a football-shaped, double-ring human mitochondrial chaperonin complex at 3.15 A, which is a novel intermediate, likely representing the complex in an early stage of dissociation. Interestingly, the mitochondrial chaperonin was captured in a state that exhibits subunit asymmetry within the rings and nucleotide symmetry between the rings. Moreover, the chaperonin tetradecamers show a different interring subunit arrangement when compared to GroEL. Our findings suggest that the mitochondrial chaperonins use a mechanism that is distinct from the mechanism of the well-studied Escherichia coli system.

Crystal structure of the human mitochondrial chaperonin symmetrical football complex.,Nisemblat S, Yaniv O, Parnas A, Frolow F, Azem A Proc Natl Acad Sci U S A. 2015 Apr 27. pii: 201411718. PMID:25918392^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nisemblat S, Yaniv O, Parnas A, Frolow F, Azem A. Crystal structure of the human mitochondrial chaperonin symmetrical football complex. Proc Natl Acad Sci U S A. 2015 Apr 27. pii: 201411718. PMID:25918392 doi:http://dx.doi.org/10.1073/pnas.1411718112

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4pj1"

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 == Publication Abstract from PubMed ==
-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.
+Human mitochondria harbor a single type I chaperonin system that is generally thought to function via a unique single-ring intermediate. To date, no crystal structure has been published for any mammalian type I chaperonin complex. In this study, we describe the crystal structure of a football-shaped, double-ring human mitochondrial chaperonin complex at 3.15 A, which is a novel intermediate, likely representing the complex in an early stage of dissociation. Interestingly, the mitochondrial chaperonin was captured in a state that exhibits subunit asymmetry within the rings and nucleotide symmetry between the rings. Moreover, the chaperonin tetradecamers show a different interring subunit arrangement when compared to GroEL. Our findings suggest that the mitochondrial chaperonins use a mechanism that is distinct from the mechanism of the well-studied Escherichia coli system.
-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<ref>PMID:24419632</ref>
+Crystal structure of the human mitochondrial chaperonin symmetrical football complex.,Nisemblat S, Yaniv O, Parnas A, Frolow F, Azem A Proc Natl Acad Sci U S A. 2015 Apr 27. pii: 201411718. PMID:25918392<ref>PMID:25918392</ref>
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

4pj1

From Proteopedia

Revision as of 06:30, 13 May 2015

Crystal structure of the human mitochondrial chaperonin symmetrical 'football' complex

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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