View source for 3izn


==Mm-cpn deltalid with ATP==
<SX load='3izn' size='340' side='right' viewer='molstar' caption='[[3izn]], [[Resolution|resolution]] 6.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3izn]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43000 Atcc 43000]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IZN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IZN FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3izh|3izh]], [[3izi|3izi]], [[3izj|3izj]], [[3izk|3izk]], [[3izl|3izl]], [[3izm|3izm]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hsp60, MMP1515 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=39152 ATCC 43000])</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=3izn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3izn OCA], [http://pdbe.org/3izn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3izn RCSB], [http://www.ebi.ac.uk/pdbsum/3izn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3izn ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Group II chaperonins are ATP-dependent ring-shaped complexes that bind nonnative polypeptides and facilitate protein folding in archaea and eukaryotes. A built-in lid encapsulates substrate proteins within the central chaperonin chamber. Here, we describe the fate of the substrate during the nucleotide cycle of group II chaperonins. The chaperonin substrate-binding sites are exposed, and the lid is open in both the ATP-free and ATP-bound prehydrolysis states. ATP hydrolysis has a dual function in the folding cycle, triggering both lid closure and substrate release into the central chamber. Notably, substrate release can occur in the absence of a lid, and lid closure can occur without substrate release. However, productive folding requires both events, so that the polypeptide is released into the confined space of the closed chamber where it folds. Our results show that ATP hydrolysis coordinates the structural and functional determinants that trigger productive folding.

Dual Action of ATP Hydrolysis Couples Lid Closure to Substrate Release into the Group II Chaperonin Chamber.,Douglas NR, Reissmann S, Zhang J, Chen B, Jakana J, Kumar R, Chiu W, Frydman J Cell. 2011 Jan 21;144(2):240-52. PMID:21241893<ref>PMID:21241893</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3izn" style="background-color:#fffaf0;"></div>

==See Also==
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
== References ==
<references/>
__TOC__
</SX>
[[Category: Atcc 43000]]
[[Category: Large Structures]]
[[Category: Chen, B]]
[[Category: Chiu, W]]
[[Category: Douglas, N R]]
[[Category: Frydman, J]]
[[Category: Jakana, J]]
[[Category: Kumar, R]]
[[Category: Reissmann, S]]
[[Category: Zhang, J]]
[[Category: Chaperone]]
[[Category: Chaperonin]]
[[Category: Maripaludi]]
[[Category: Mm-cpn]]