3ruq: Difference between revisions

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==Crystal structure of Cpn-WT in complex with ADP from Methanococcus maripaludis==
==Crystal structure of Cpn-WT in complex with ADP from Methanococcus maripaludis==
<StructureSection load='3ruq' size='340' side='right' caption='[[3ruq]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='3ruq' size='340' side='right'caption='[[3ruq]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ruq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanococcus_maripaludis Methanococcus maripaludis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RUQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RUQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ruq]] is a 4 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=3RUQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RUQ 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">X-ray diffraction, [[Resolution|Resolution]] 2.798&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3kfb|3kfb]], [[3kfe|3kfe]], [[3kfk|3kfk]], [[3rus|3rus]], [[3ruv|3ruv]], [[3ruw|3ruw]]</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=3ruq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ruq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ruq RCSB], [http://www.ebi.ac.uk/pdbsum/3ruq PDBsum]</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=3ruq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ruq OCA], [https://pdbe.org/3ruq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ruq RCSB], [https://www.ebi.ac.uk/pdbsum/3ruq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ruq ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q877G8_METMI Q877G8_METMI]
Group II chaperonins mediate protein folding in an ATP-dependent manner in eukaryotes and archaea. The binding of ATP and subsequent hydrolysis promotes the closure of the multi-subunit rings where protein folding occurs. The mechanism by which local changes in the nucleotide-binding site are communicated between individual subunits is unknown. The crystal structure of the archaeal chaperonin from Methanococcus maripaludis in several nucleotides bound states reveals the local conformational changes associated with ATP hydrolysis. Residue Lys-161, which is extremely conserved among group II chaperonins, forms interactions with the gamma-phosphate of ATP but shows a different orientation in the presence of ADP. The loss of the ATP gamma-phosphate interaction with Lys-161 in the ADP state promotes a significant rearrangement of a loop consisting of residues 160-169. We propose that Lys-161 functions as an ATP sensor and that 160-169 constitutes a nucleotide-sensing loop (NSL) that monitors the presence of the gamma-phosphate. Functional analysis using NSL mutants shows a significant decrease in ATPase activity, suggesting that the NSL is involved in timing of the protein folding cycle.
 
Mechanism of nucleotide sensing in group II chaperonins.,Pereira JH, Ralston CY, Douglas NR, Kumar R, Lopez T, McAndrew RP, Knee KM, King JA, Frydman J, Adams PD EMBO J. 2011 Dec 23. doi: 10.1038/emboj.2011.468. PMID:22193720<ref>PMID:22193720</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Chaperonin|Chaperonin]]
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanococcus maripaludis]]
[[Category: Methanococcus maripaludis]]
[[Category: Adams, P D]]
[[Category: Adams PD]]
[[Category: Douglas, N R]]
[[Category: Douglas NR]]
[[Category: Frydman, J]]
[[Category: Frydman J]]
[[Category: Knee, K M]]
[[Category: Knee KM]]
[[Category: Kumar, R]]
[[Category: Kumar R]]
[[Category: McAndrew, R P]]
[[Category: McAndrew RP]]
[[Category: Pereira, J H]]
[[Category: Pereira JH]]
[[Category: Ralston, C Y]]
[[Category: Ralston CY]]
[[Category: Atp binding]]
[[Category: Chaperone]]
[[Category: Double-ring]]
[[Category: Group ii chaperonin]]
[[Category: Protein folding machinery]]

Latest revision as of 15:38, 14 March 2024

Crystal structure of Cpn-WT in complex with ADP from Methanococcus maripaludisCrystal structure of Cpn-WT in complex with ADP from Methanococcus maripaludis

Structural highlights

3ruq is a 4 chain structure with sequence from Methanococcus maripaludis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.798Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q877G8_METMI

See Also

3ruq, resolution 2.80Å

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