8ba8: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 8ba8 is ~~ON HOLD~~

==CryoEM structure of GroEL-ADP.BeF3-Rubisco.==

== Structural highlights ==

<table><tr><td colspan='2'>[[8ba8]] 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=8BA8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BA8 FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4Å</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=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=8ba8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ba8 OCA], [https://pdbe.org/8ba8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ba8 RCSB], [https://www.ebi.ac.uk/pdbsum/8ba8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ba8 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]

== Publication Abstract from PubMed ==

The bacterial chaperonin GroEL-GroES promotes protein folding through ATP-regulated cycles of substrate protein binding, encapsulation, and release. Here, we have used cryoEM to determine structures of GroEL, GroEL-ADP.BeF(3), and GroEL-ADP.AlF(3)-GroES all complexed with the model substrate Rubisco. Our structures provide a series of snapshots that show how the conformation and interactions of non-native Rubisco change as it proceeds through the GroEL-GroES reaction cycle. We observe specific charged and hydrophobic GroEL residues forming strong initial contacts with non-native Rubisco. Binding of ATP or ADP.BeF(3) to GroEL-Rubisco results in the formation of an intermediate GroEL complex displaying striking asymmetry in the ATP/ADP.BeF(3)-bound ring. In this ring, four GroEL subunits bind Rubisco and the other three are in the GroES-accepting conformation, suggesting how GroEL can recruit GroES without releasing bound substrate. Our cryoEM structures of stalled GroEL-ADP.AlF(3)-Rubisco-GroES complexes show Rubisco folding intermediates interacting with GroEL-GroES via different sets of residues.

~~Authors:~~ Gardner, S., ~~Saibil, H~~.R.

Structural basis of substrate progression through the bacterial chaperonin cycle.,Gardner S, Darrow MC, Lukoyanova N, Thalassinos K, Saibil HR Proc Natl Acad Sci U S A. 2023 Dec 12;120(50):e2308933120. doi: , 10.1073/pnas.2308933120. Epub 2023 Dec 8. PMID:38064510<ref>PMID:38064510</ref>

~~Description: CryoEM structure~~ of ~~GroEL~~-~~ADP.BeF3~~-~~Rubisco.~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

[[Category: Gardner, S]]

[[Category: Saibil~~, H.R~~]]

== References ==

__TOC__

</StructureSection>

[[Category: Escherichia coli K-12]]

[[Category: Large Structures]]

[[Category: Gardner S]]

[[Category: Saibil HR]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8ba8 is ON HOLD
+==CryoEM structure of GroEL-ADP.BeF3-Rubisco.==
+<StructureSection load='8ba8' size='340' side='right'caption='[[8ba8]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8ba8]] 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=8BA8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BA8 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4&#8491;</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=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=8ba8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ba8 OCA], [https://pdbe.org/8ba8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ba8 RCSB], [https://www.ebi.ac.uk/pdbsum/8ba8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ba8 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-GroES promotes protein folding through ATP-regulated cycles of substrate protein binding, encapsulation, and release. Here, we have used cryoEM to determine structures of GroEL, GroEL-ADP.BeF(3), and GroEL-ADP.AlF(3)-GroES all complexed with the model substrate Rubisco. Our structures provide a series of snapshots that show how the conformation and interactions of non-native Rubisco change as it proceeds through the GroEL-GroES reaction cycle. We observe specific charged and hydrophobic GroEL residues forming strong initial contacts with non-native Rubisco. Binding of ATP or ADP.BeF(3) to GroEL-Rubisco results in the formation of an intermediate GroEL complex displaying striking asymmetry in the ATP/ADP.BeF(3)-bound ring. In this ring, four GroEL subunits bind Rubisco and the other three are in the GroES-accepting conformation, suggesting how GroEL can recruit GroES without releasing bound substrate. Our cryoEM structures of stalled GroEL-ADP.AlF(3)-Rubisco-GroES complexes show Rubisco folding intermediates interacting with GroEL-GroES via different sets of residues.
-Authors: Gardner, S., Saibil, H.R.
+Structural basis of substrate progression through the bacterial chaperonin cycle.,Gardner S, Darrow MC, Lukoyanova N, Thalassinos K, Saibil HR Proc Natl Acad Sci U S A. 2023 Dec 12;120(50):e2308933120. doi: , 10.1073/pnas.2308933120. Epub 2023 Dec 8. PMID:38064510<ref>PMID:38064510</ref>
-Description: CryoEM structure of GroEL-ADP.BeF3-Rubisco.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Gardner, S]]
+<div class="pdbe-citations 8ba8" style="background-color:#fffaf0;"></div>
-[[Category: Saibil, H.R]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia coli K-12]]
+[[Category: Large Structures]]
+[[Category: Gardner S]]
+[[Category: Saibil HR]]