View source for 7eux


==Crystal structure of the Lon-like protease MtaLonC with D581A mutation in complex with substrate polypeptide==
<StructureSection load='7eux' size='340' side='right'caption='[[7eux]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7eux]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Meiothermus_taiwanensis Meiothermus taiwanensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EUX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EUX 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]] 2.25&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=7eux FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eux OCA], [https://pdbe.org/7eux PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eux RCSB], [https://www.ebi.ac.uk/pdbsum/7eux PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eux ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C9DRU9_9DEIN C9DRU9_9DEIN] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7eux" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Meiothermus taiwanensis]]
[[Category: Chang CI]]
[[Category: Hsieh KY]]
[[Category: Huang KF]]
[[Category: Kuo CI]]
[[Category: Su SC]]