7rak: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='7rak' size='340' side='right'caption='[[7rak]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
<StructureSection load='7rak' size='340' side='right'caption='[[7rak]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.9&#8491;</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;">
== Publication Abstract from PubMed ==
Chaperonins 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<ref>PMID:34362932</ref>
==See Also==
 
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7rak" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Methanococcus maripaludis]]
[[Category: Chiu W]]
[[Category: Chiu W]]
[[Category: Frydman J]]
[[Category: Frydman J]]
[[Category: Schmid M]]
[[Category: Schmid M]]
[[Category: Zhao Y]]
[[Category: Zhao Y]]

Latest revision as of 08:46, 5 June 2024

Methanococcus maripaludis chaperonin complex in open conformationMethanococcus maripaludis chaperonin complex in open conformation

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

See Also

7rak, resolution 3.90Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=7rak&oldid=4231318"