3aei

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Current revision (08:40, 7 February 2024) (edit) (undo)
 
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<StructureSection load='3aei' size='340' side='right'caption='[[3aei]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='3aei' size='340' side='right'caption='[[3aei]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3aei]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AEI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AEI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3aei]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_sp._JCM_11816 Thermococcus sp. JCM 11816]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AEI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AEI 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.7&#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;'>[[2zqm|2zqm]], [[2zdi|2zdi]]</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3aei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aei OCA], [https://pdbe.org/3aei PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aei RCSB], [https://www.ebi.ac.uk/pdbsum/3aei PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aei 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=3aei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aei OCA], [https://pdbe.org/3aei PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aei RCSB], [https://www.ebi.ac.uk/pdbsum/3aei PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aei 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/B0I3E2_THEK1 B0I3E2_THEK1]
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Prefoldin (PFD) is a hexameric chaperone that captures a protein substrate and transfers it to a group II chaperonin (CPN) to complete protein folding. We have studied the interaction between PFD and CPN using those from a hyperthermophilic archaeon, Thermococcus strain KS-1 (T. KS-1). In this study, we determined the crystal structure of the T. KS-1 PFDbeta2 subunit and characterized the interactions between T. KS-1 CPNs (CPNalpha and CPNbeta) and T. KS-1 PFDs (PFDalpha1-beta1 and PFDalpha2-beta2). As predicted from its amino acid sequence, the PFDbeta2 subunit conforms to a structure similar to those of the PFDbeta1 subunit and the Pyrococcus horikoshii OT3 PFDbeta subunit, with the exception of the tip of its coiled-coil domain, which is thought to be the CPN interaction site. The interactions between T. KS-1 CPNs and PFDs (CPNalpha and PFDalpha1-beta1; CPNalpha and PFDalpha2-beta2; CPNbeta and PFDalpha1-beta1; and CPNbeta and PFDalpha2-beta2) were analyzed using the Biacore T100 system at various temperatures ranging from 20 to 45 degrees C. The affinities between PFDs and CPNs increased with an increase in temperature. The thermodynamic parameters calculated from association constants showed that the interaction between PFD and CPN is entropy driven. Among the four combinations of PFD-CPN interactions, the entropy difference in binding between CPNbeta and PFDalpha2-beta2 was the largest, and affinity significantly increased at higher temperatures. Considering that expression of PFDalpha2-beta2 and CPNbeta subunit is induced upon heat shock, our results suggest that PFDalpha1-beta1 is a general PFD for T. KS-1 CPNs, whereas PFDalpha2-beta2 is specific for CPNbeta.
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Thermodynamic characterization of the interaction between prefoldin and group II chaperonin.,Sahlan M, Zako T, Tai PT, Ohtaki A, Noguchi K, Maeda M, Miyatake H, Dohmae N, Yohda M J Mol Biol. 2010 Jun 18;399(4):628-36. Epub 2010 Apr 29. PMID:20434454<ref>PMID:20434454</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 3aei" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Miyatake, H]]
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[[Category: Thermococcus sp. JCM 11816]]
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[[Category: Noguchi, K]]
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[[Category: Miyatake H]]
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[[Category: Ohtaki, A]]
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[[Category: Noguchi K]]
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[[Category: Sato, T]]
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[[Category: Ohtaki A]]
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[[Category: Sugano, Y]]
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[[Category: Sato T]]
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[[Category: Yohda, M]]
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[[Category: Sugano Y]]
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[[Category: Chaperone]]
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[[Category: Yohda M]]
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[[Category: Coiled coil]]
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[[Category: Double helix]]
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Current revision

Crystal structure of the prefoldin beta2 subunit from Thermococcus strain KS-1

PDB ID 3aei

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