7fie: Difference between revisions
New page: '''Unreleased structure''' The entry 7fie is ON HOLD Authors: Description: Category: Unreleased Structures |
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The | ==Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex (conformation 2)== | ||
<StructureSection load='7fie' size='340' side='right'caption='[[7fie]], [[Resolution|resolution]] 2.36Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7fie]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Meiothermus_taiwanensis Meiothermus taiwanensis] and [https://en.wikipedia.org/wiki/Meiothermus_taiwanensis_WR-220 Meiothermus taiwanensis WR-220]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7FIE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FIE FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.36Å</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=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</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=7fie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fie OCA], [https://pdbe.org/7fie PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fie RCSB], [https://www.ebi.ac.uk/pdbsum/7fie PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fie ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Lon protease is the prototype of a family of proteolytic machines with adenosine triphosphatase modules built into a substrate degradation chamber. Lon is known to degrade protein substrates in a processive fashion, cutting a protein chain processively into small peptides before commencing cleavages of another protein chain. Here, we present structural and biochemical evidence demonstrating that processive substrate degradation occurs at each of the six proteolytic active sites of Lon, which forms a deep groove that partially encloses the substrate polypeptide chain by accommodating only the unprimed residues and permits processive cleavage in the C-to-N direction. We identify a universally conserved acidic residue at the exit side of the binding groove indispensable for the proteolytic activity. This noncatalytic residue likely promotes processive proteolysis by carboxyl-carboxylate interactions with cleaved intermediates. Together, these results uncover a previously unrecognized mechanism for processive substrate degradation by the Lon protease. | |||
Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex.,Li S, Hsieh KY, Kuo CI, Su SC, Huang KF, Zhang K, Chang CI Sci Adv. 2021 Nov 12;7(46):eabj9537. doi: 10.1126/sciadv.abj9537. Epub 2021 Nov , 10. PMID:34757797<ref>PMID:34757797</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7fie" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Meiothermus taiwanensis]] | |||
[[Category: Meiothermus taiwanensis WR-220]] | |||
[[Category: Chang CI]] | |||
[[Category: Hsieh K]] | |||
[[Category: Huang K]] | |||
[[Category: Kuo C]] | |||
[[Category: Li S]] | |||
[[Category: Su S]] | |||
[[Category: Zhang K]] | |||
Latest revision as of 08:10, 12 June 2024
Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex (conformation 2)Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex (conformation 2)
Structural highlights
Publication Abstract from PubMedThe Lon protease is the prototype of a family of proteolytic machines with adenosine triphosphatase modules built into a substrate degradation chamber. Lon is known to degrade protein substrates in a processive fashion, cutting a protein chain processively into small peptides before commencing cleavages of another protein chain. Here, we present structural and biochemical evidence demonstrating that processive substrate degradation occurs at each of the six proteolytic active sites of Lon, which forms a deep groove that partially encloses the substrate polypeptide chain by accommodating only the unprimed residues and permits processive cleavage in the C-to-N direction. We identify a universally conserved acidic residue at the exit side of the binding groove indispensable for the proteolytic activity. This noncatalytic residue likely promotes processive proteolysis by carboxyl-carboxylate interactions with cleaved intermediates. Together, these results uncover a previously unrecognized mechanism for processive substrate degradation by the Lon protease. Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex.,Li S, Hsieh KY, Kuo CI, Su SC, Huang KF, Zhang K, Chang CI Sci Adv. 2021 Nov 12;7(46):eabj9537. doi: 10.1126/sciadv.abj9537. Epub 2021 Nov , 10. PMID:34757797[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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