7rak: Difference between revisions
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<StructureSection load='7rak' size='340' side='right'caption='[[7rak]], [[Resolution|resolution]] 3.90Å' scene=''> | <StructureSection load='7rak' size='340' side='right'caption='[[7rak]], [[Resolution|resolution]] 3.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7rak]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[7rak]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanococcus_maripaludis Methanococcus maripaludis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RAK FirstGlance]. <br> | ||
</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></td></tr> | </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></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=7rak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rak OCA], [https://pdbe.org/7rak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rak RCSB], [https://www.ebi.ac.uk/pdbsum/7rak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rak 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=7rak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rak OCA], [https://pdbe.org/7rak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rak RCSB], [https://www.ebi.ac.uk/pdbsum/7rak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rak ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q877G8_METMI Q877G8_METMI] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chiu | [[Category: Methanococcus maripaludis]] | ||
[[Category: Frydman | [[Category: Chiu W]] | ||
[[Category: Schmid | [[Category: Frydman J]] | ||
[[Category: Zhao | [[Category: Schmid M]] | ||
[[Category: Zhao Y]] | |||
Revision as of 07:36, 30 September 2022
Methanococcus maripaludis chaperonin complex in open conformationMethanococcus maripaludis chaperonin complex in open conformation
Structural highlights
FunctionPublication Abstract from PubMedChaperonins are homo- or hetero-oligomeric complexes that use ATP binding and hydrolysis to facilitate protein folding. ATP hydrolysis exhibits both positive and negative cooperativity. The mechanism by which chaperonins coordinate ATP utilization in their multiple subunits remains unclear. Here we use cryoEM to study ATP binding in the homo-oligomeric archaeal chaperonin from Methanococcus maripaludis (MmCpn), consisting of two stacked rings composed of eight identical subunits each. Using a series of image classification steps, we obtained different structural snapshots of individual chaperonins undergoing the nucleotide binding process. We identified nucleotide-bound and free states of individual subunits in each chaperonin, allowing us to determine the ATP occupancy state of each MmCpn particle. We observe distinctive tertiary and quaternary structures reflecting variations in nucleotide occupancy and subunit conformations in each chaperonin complex. Detailed analysis of the nucleotide distribution in each MmCpn complex indicates that individual ATP binding events occur in a statistically random manner for MmCpn, both within and across the rings. Our findings illustrate the power of cryoEM to characterize a biochemical property of multi-subunit ligand binding cooperativity at the individual particle level. CryoEM reveals the stochastic nature of individual ATP binding events in a group II chaperonin.,Zhao Y, Schmid MF, Frydman J, Chiu W Nat Commun. 2021 Aug 6;12(1):4754. doi: 10.1038/s41467-021-25099-0. PMID:34362932[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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