4pj1

From Proteopedia

(Difference between revisions)

Revision as of 08:41, 22 November 2017

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

Structural highlights

4pj1 is a 28 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	HSPD1, HSP60 (HUMAN), HSPE1 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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"

@@ Line 3: / Line 3: @@
 <StructureSection load='4pj1' size='340' side='right' caption='[[4pj1]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4pj1]] is a 28 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PJ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PJ1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4pj1]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PJ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PJ1 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSPD1, HSP60 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), HSPE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pj1 OCA], [http://pdbe.org/4pj1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pj1 RCSB], [http://www.ebi.ac.uk/pdbsum/4pj1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pj1 ProSAT]</span></td></tr>
 </table>
@@ Line 24: / Line 25: @@
 __TOC__
 </StructureSection>
+[[Category: Human]]
 [[Category: Azem, A]]
 [[Category: Frolow, F]]
@@ Line 30: / Line 32: @@
 [[Category: Chaperonin]]
 [[Category: Complex]]
-[[Category: Human]]
 [[Category: Mitochondrial]]
 [[Category: Symmetric]]

4pj1

From Proteopedia

Revision as of 08:41, 22 November 2017

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?)

Views

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