View source for 6pxk


==3.65 Angstroms resolution structure of HslU with an axial-channel plug==
<StructureSection load='6pxk' size='340' side='right'caption='[[6pxk]], [[Resolution|resolution]] 3.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6pxk]] is a 13 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=6PXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PXK FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.647&#8491;</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=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=6pxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pxk OCA], [https://pdbe.org/6pxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pxk RCSB], [https://www.ebi.ac.uk/pdbsum/6pxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pxk ProSAT]</span></td></tr>
</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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6pxk" style="background-color:#fffaf0;"></div>

==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Baytshtok V]]
[[Category: Grant RA]]
[[Category: Sauer RT]]