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| | ==Visualizing GroEL-ES in the Act of Encapsulating a Non-Native Substrate Protein== | | ==Visualizing GroEL-ES in the Act of Encapsulating a Non-Native Substrate Protein== |
| - | <StructureSection load='3zq0' size='340' side='right' caption='[[3zq0]], [[Resolution|resolution]] 9.20Å' scene=''> | + | <SX load='3zq0' size='340' side='right' viewer='molstar' caption='[[3zq0]], [[Resolution|resolution]] 9.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3zq0]] is a 21 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecobb Ecobb] and [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZQ0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZQ0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3zq0]] is a 21 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21 Escherichia coli BL21] and [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=3ZQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZQ0 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">Electron Microscopy, [[Resolution|Resolution]] 9.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zpz|3zpz]], [[3zq1|3zq1]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3zq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zq0 OCA], [http://pdbe.org/3zq0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zq0 RCSB], [http://www.ebi.ac.uk/pdbsum/3zq0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zq0 ProSAT]</span></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=3zq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zq0 OCA], [https://pdbe.org/3zq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zq0 RCSB], [https://www.ebi.ac.uk/pdbsum/3zq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zq0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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] [[http://www.uniprot.org/uniprot/CH10_ECOLI CH10_ECOLI]] Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.[HAMAP-Rule:MF_00580] | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 3zq0" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3zq0" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Chaperonin 3D structures|Chaperonin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| - | </StructureSection> | + | </SX> |
| - | [[Category: Ecobb]] | + | [[Category: Escherichia coli BL21]] |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Chen, D H]] | + | [[Category: Large Structures]] |
| - | [[Category: Chiu, W]] | + | [[Category: Chen D-H]] |
| - | [[Category: Lin, Z]] | + | [[Category: Chiu W]] |
| - | [[Category: Madan, D]] | + | [[Category: Lin Z]] |
| - | [[Category: Rye, H S]] | + | [[Category: Madan D]] |
| - | [[Category: Schroder, G F]] | + | [[Category: Rye HS]] |
| - | [[Category: Weaver, J]] | + | [[Category: Schroder GF]] |
| - | [[Category: Encapsulation]]
| + | [[Category: Weaver J]] |
| - | [[Category: Heterogeneity]]
| + | |
| - | [[Category: Protein folding]]
| + | |
| Structural highlights
Function
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]
Publication Abstract from PubMed
The GroEL/ES chaperonin system is required for the assisted folding of many proteins. How these substrate proteins are encapsulated within the GroEL-GroES cavity is poorly understood. Using symmetry-free, single-particle cryo-electron microscopy, we have characterized a chemically modified mutant of GroEL (EL43Py) that is trapped at a normally transient stage of substrate protein encapsulation. We show that the symmetric pattern of the GroEL subunits is broken as the GroEL cis-ring apical domains reorient to accommodate the simultaneous binding of GroES and an incompletely folded substrate protein (RuBisCO). The collapsed RuBisCO folding intermediate binds to the lower segment of two apical domains, as well as to the normally unstructured GroEL C-terminal tails. A comparative structural analysis suggests that the allosteric transitions leading to substrate protein release and folding involve concerted shifts of GroES and the GroEL apical domains and C-terminal tails.
Visualizing GroEL/ES in the Act of Encapsulating a Folding Protein.,Chen DH, Madan D, Weaver J, Lin Z, Schroder GF, Chiu W, Rye HS Cell. 2013 Jun 6;153(6):1354-65. doi: 10.1016/j.cell.2013.04.052. PMID:23746846[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chen DH, Madan D, Weaver J, Lin Z, Schroder GF, Chiu W, Rye HS. Visualizing GroEL/ES in the Act of Encapsulating a Folding Protein. Cell. 2013 Jun 6;153(6):1354-65. doi: 10.1016/j.cell.2013.04.052. PMID:23746846 doi:10.1016/j.cell.2013.04.052
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