3ruq

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Current revision (12:38, 14 March 2024) (edit) (undo)
 
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<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 ==
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<table><tr><td colspan='2'>[[3ruq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43000 Atcc 43000]. 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>
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<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>
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</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>
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</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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3kfb|3kfb]], [[3kfe|3kfe]], [[3kfk|3kfk]], [[3rus|3rus]], [[3ruv|3ruv]], [[3ruw|3ruw]]</div></td></tr>
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<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'>[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>
<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>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q877G8_METMI Q877G8_METMI]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3ruq" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
*[[Chaperonin 3D structures|Chaperonin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 43000]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Adams, P D]]
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[[Category: Methanococcus maripaludis]]
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[[Category: Douglas, N R]]
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[[Category: Adams PD]]
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[[Category: Frydman, J]]
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[[Category: Douglas NR]]
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[[Category: Knee, K M]]
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[[Category: Frydman J]]
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[[Category: Kumar, R]]
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[[Category: Knee KM]]
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[[Category: McAndrew, R P]]
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[[Category: Kumar R]]
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[[Category: Pereira, J H]]
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[[Category: McAndrew RP]]
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[[Category: Ralston, C Y]]
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[[Category: Pereira JH]]
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[[Category: Atp binding]]
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[[Category: Ralston CY]]
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[[Category: Chaperone]]
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[[Category: Double-ring]]
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[[Category: Group ii chaperonin]]
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[[Category: Protein folding machinery]]
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Current revision

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

PDB ID 3ruq

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