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==3.74 Angstroms resolution structure of HlsU with an axial-channel plug== | ==3.74 Angstroms resolution structure of HlsU with an axial-channel plug== | ||
<StructureSection load='6pxl' size='340' side='right'caption='[[6pxl]]' scene=''> | <StructureSection load='6pxl' size='340' side='right'caption='[[6pxl]], [[Resolution|resolution]] 3.74Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PXL OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6pxl]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PXL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PXL FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.741Å</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>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=6pxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pxl OCA], [https://pdbe.org/6pxl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pxl RCSB], [https://www.ebi.ac.uk/pdbsum/6pxl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pxl ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/HSLU_ECOLI HSLU_ECOLI] ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.<ref>PMID:8662828</ref> <ref>PMID:8650174</ref> <ref>PMID:9288941</ref> <ref>PMID:9393683</ref> <ref>PMID:10452560</ref> <ref>PMID:10419524</ref> <ref>PMID:15696175</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
At low temperatures, protein degradation by the AAA+ HslUV protease is very slow. New crystal structures reveal that residues in the intermediate domain of the HslU(6) unfoldase can plug its axial channel, blocking productive substrate binding and subsequent unfolding, translocation, and degradation by the HslV(12) peptidase. Biochemical experiments with wild-type and mutant enzymes support a model in which heat-induced melting of this autoinhibitory plug activates HslUV proteolysis. | |||
Heat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug.,Baytshtok V, Fei X, Shih TT, Grant RA, Santos JC, Baker TA, Sauer RT Cell Rep. 2021 Jan 19;34(3):108639. doi: 10.1016/j.celrep.2020.108639. PMID:33472065<ref>PMID:33472065</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6pxl" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[ATPase 3D structures|ATPase 3D structures]] | |||
*[[Heat Shock Protein structures|Heat Shock Protein structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Baytshtok V]] | [[Category: Baytshtok V]] | ||
[[Category: Grant RA]] | [[Category: Grant RA]] | ||
[[Category: Sauer RT]] | [[Category: Sauer RT]] | ||
Revision as of 10:37, 11 October 2023
3.74 Angstroms resolution structure of HlsU with an axial-channel plug3.74 Angstroms resolution structure of HlsU with an axial-channel plug
Structural highlights
FunctionHSLU_ECOLI ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.[1] [2] [3] [4] [5] [6] [7] Publication Abstract from PubMedAt low temperatures, protein degradation by the AAA+ HslUV protease is very slow. New crystal structures reveal that residues in the intermediate domain of the HslU(6) unfoldase can plug its axial channel, blocking productive substrate binding and subsequent unfolding, translocation, and degradation by the HslV(12) peptidase. Biochemical experiments with wild-type and mutant enzymes support a model in which heat-induced melting of this autoinhibitory plug activates HslUV proteolysis. Heat activates the AAA+ HslUV protease by melting an axial autoinhibitory plug.,Baytshtok V, Fei X, Shih TT, Grant RA, Santos JC, Baker TA, Sauer RT Cell Rep. 2021 Jan 19;34(3):108639. doi: 10.1016/j.celrep.2020.108639. PMID:33472065[8] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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