6tmt

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Current revision (13:05, 24 January 2024) (edit) (undo)
 
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<StructureSection load='6tmt' size='340' side='right'caption='[[6tmt]], [[Resolution|resolution]] 4.03&Aring;' scene=''>
<StructureSection load='6tmt' size='340' side='right'caption='[[6tmt]], [[Resolution|resolution]] 4.03&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6tmt]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_phage_el Pseudomonas phage el]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TMT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TMT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6tmt]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_phage_EL Pseudomonas phage EL]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TMT 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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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]] 4.03&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6tmt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tmt OCA], [http://pdbe.org/6tmt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tmt RCSB], [http://www.ebi.ac.uk/pdbsum/6tmt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tmt ProSAT]</span></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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6tmt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tmt OCA], [https://pdbe.org/6tmt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tmt RCSB], [https://www.ebi.ac.uk/pdbsum/6tmt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tmt 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/Q2Z0T5_9CAUD Q2Z0T5_9CAUD]
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Chaperonins are ubiquitous molecular chaperones found in all domains of life. They form ring-shaped complexes that assist in the folding of substrate proteins in an ATP-dependent reaction cycle. Key to the folding cycle is the transient encapsulation of substrate proteins by the chaperonin. Here we present a structural and functional characterization of the chaperonin gp146 (EL) from the phage EL of Pseudomonas aeruginosa. EL, an evolutionarily distant homolog of bacterial GroEL, is active in ATP hydrolysis and prevents the aggregation of denatured protein in a nucleotide-dependent manner. However, EL failed to refold the encapsulation-dependent model substrate rhodanese and did not interact with E. coli GroES, the lid-shaped co-chaperone of GroEL. EL forms tetradecameric double-ring complexes, which dissociate into single rings in the presence of ATP. Crystal structures of EL (at 3.54 and 4.03 A) in presence of ATP*BeFx revealed two distinct single-ring conformational states, both with open access to the ring cavity. One state showed uniform ATP-bound subunit conformations (symmetric state), whereas the second combined distinct ATP- and ADP-bound subunit conformations (asymmetric state). Cryo-electron microscopy of apo-EL revealed a double-ring structure composed of rings in the asymmetric state (3.45 A resolution). We propose that the phage chaperonin undergoes nucleotide-dependent conformational switching between double- and single rings and functions in aggregation prevention without substrate protein encapsulation. Thus, EL may represent an evolutionarily more ancient chaperonin prior to acquisition of the encapsulation mechanism.
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Structure and conformational cycle of a bacteriophage-encoded chaperonin.,Bracher A, Paul SS, Wang H, Wischnewski N, Hartl FU, Hayer-Hartl M PLoS One. 2020 Apr 27;15(4):e0230090. doi: 10.1371/journal.pone.0230090., eCollection 2020. PMID:32339190<ref>PMID:32339190</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 6tmt" 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: Pseudomonas phage el]]
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[[Category: Pseudomonas phage EL]]
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[[Category: Bracher, A]]
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[[Category: Bracher A]]
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[[Category: Hartl, F U]]
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[[Category: Hartl FU]]
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[[Category: Hayer-Hartl, M]]
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[[Category: Hayer-Hartl M]]
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[[Category: Paul, S S]]
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[[Category: Paul SS]]
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[[Category: Wang, H]]
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[[Category: Wang H]]
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[[Category: Wischnewski, N]]
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[[Category: Wischnewski N]]
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[[Category: Atpase]]
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[[Category: Chaperone]]
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[[Category: Chaperonin]]
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[[Category: Molecular chaperone]]
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Current revision

Crystal structure of the chaperonin gp146 from the bacteriophage EL 2 (Pseudomonas aeruginosa) in presence of ATP-BeFx, crystal form I

PDB ID 6tmt

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OCA

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