4pj1: Difference between revisions

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 ==Crystal structure of the human mitochondrial chaperonin symmetrical 'football' complex==
-<StructureSection load='4pj1' size='340' side='right' caption='[[4pj1]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
+<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 [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.15&#8491;</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://www.rcsb.org/pdb/explore.do?structureId=4pj1 RCSB], [http://www.ebi.ac.uk/pdbsum/4pj1 PDBsum]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4pj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pj1 OCA], [https://pdbe.org/4pj1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pj1 RCSB], [https://www.ebi.ac.uk/pdbsum/4pj1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pj1 ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/CH60_HUMAN 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.
+[https://www.uniprot.org/uniprot/CH60_HUMAN 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 ==
-[[http://www.uniprot.org/uniprot/CH60_HUMAN 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. [[http://www.uniprot.org/uniprot/CH10_HUMAN 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.
+[https://www.uniprot.org/uniprot/CH60_HUMAN 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.
 <div style="background-color:#fffaf0;">
 == 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>
 </div>
+<div class="pdbe-citations 4pj1" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Azem, A]]
+[[Category: Homo sapiens]]
-[[Category: Frolow, F]]
+[[Category: Large Structures]]
-[[Category: Nisemblat, S]]
+[[Category: Azem A]]
-[[Category: Chaperone]]
+[[Category: Frolow F]]
-[[Category: Chaperonin]]
+[[Category: Nisemblat S]]
-[[Category: Complex]]
-[[Category: Human]]
-[[Category: Mitochondrial]]
-[[Category: Symmetric]]