View source for 5opw


==Crystal structure of the GroEL mutant A109C==
<StructureSection load='5opw' size='340' side='right'caption='[[5opw]], [[Resolution|resolution]] 3.19&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5opw]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OPW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OPW 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]] 3.19&#8491;</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=5opw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5opw OCA], [https://pdbe.org/5opw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5opw RCSB], [https://www.ebi.ac.uk/pdbsum/5opw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5opw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CH60_ECOLI CH60_ECOLI] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.[HAMAP-Rule:MF_00600]  Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.[HAMAP-Rule:MF_00600]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The bacterial chaperonin GroEL and its cofactor, GroES, form a nano-cage for a single molecule of substrate protein (SP) to fold in isolation. GroEL and GroES undergo an ATP-regulated interaction cycle to close and open the folding cage. GroEL consists of two heptameric rings stacked back to back. Here, we show that GroEL undergoes transient ring separation, resulting in ring exchange between complexes. Ring separation occurs upon ATP-binding to the trans ring of the asymmetric GroEL:7ADP:GroES complex in the presence or absence of SP and is a consequence of inter-ring negative allostery. We find that a GroEL mutant unable to perform ring separation is folding active but populates symmetric GroEL:GroES2 complexes, where both GroEL rings function simultaneously rather than sequentially. As a consequence, SP binding and release from the folding chamber is inefficient, and E. coli growth is impaired. We suggest that transient ring separation is an integral part of the chaperonin mechanism.

GroEL Ring Separation and Exchange in the Chaperonin Reaction.,Yan X, Shi Q, Bracher A, Milicic G, Singh AK, Hartl FU, Hayer-Hartl M Cell. 2017 Dec 26. pii: S0092-8674(17)31490-3. doi: 10.1016/j.cell.2017.12.010. PMID:29336887<ref>PMID:29336887</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5opw" style="background-color:#fffaf0;"></div>

==See Also==
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Bracher A]]
[[Category: Hartl FU]]
[[Category: Hayer-Hartl M]]
[[Category: Milicic G]]
[[Category: Shi Q]]
[[Category: Singh AK]]
[[Category: Yan X]]