View source for 7k3z


==P. falciparum Cpn60 D474A mutant bound to ATP==
<StructureSection load='7k3z' size='340' side='right'caption='[[7k3z]], [[Resolution|resolution]] 3.69&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7k3z]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K3Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K3Z FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.69&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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=7k3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k3z OCA], [https://pdbe.org/7k3z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k3z RCSB], [https://www.ebi.ac.uk/pdbsum/7k3z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k3z ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8I0V3_PLAF7 Q8I0V3_PLAF7] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Plasmodium falciparum harbors group 1 and group 2 chaperonin systems to mediate the folding of cellular proteins in different cellular locations. Two distinct group 1 chaperonins operate in the organelles of mitochondria and apicoplasts, while group 2 chaperonins function in the cytosol. No structural information has been reported for any chaperonin from plasmodium. In this study, we describe the crystal structure of a double heptameric ring Plasmodium falciparum mitochondrial chaperonin 60 (Cpn60) bound with ATP, which differs significantly from any known crystal structure of chaperonin 60. The structure likely represents a unique intermediate state during conformational conversion from the closed state to the opened state. Three of the seven apical domains are highly dynamic while the equatorial domains form a stable ring. The structure implies large movements of the apical domain in the solution play a role in nucleotide-dependent regulation of substrate binding and folding. A unique 26-27 residue insertion in the equatorial domain of Plasmodium falciparum mitochondrial chaperonin greatly increases both inter-ring and intra-ring subunit-subunit interactions. The present structure provides new insights into the mechanism of Cpn60 in chaperonin assembly and function.

Crystal structure of P. falciparum Cpn60 bound to ATP reveals an open dynamic conformation before substrate binding.,Nguyen B, Ma R, Tang WK, Shi D, Tolia NH Sci Rep. 2021 Mar 15;11(1):5930. doi: 10.1038/s41598-021-85197-3. PMID:33723304<ref>PMID:33723304</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7k3z" style="background-color:#fffaf0;"></div>

==See Also==
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Plasmodium falciparum 3D7]]
[[Category: Nguyen B]]
[[Category: Shi D]]
[[Category: Tolia NH]]