View source for 6wqh


==Molecular basis for the ATPase-powered substrate translocation by the Lon AAA+ protease==
<StructureSection load='6wqh' size='340' side='right'caption='[[6wqh]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6wqh]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] 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=6WQH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WQH 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]] 3.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4KZ:N-[(1R)-1-(DIHYDROXYBORANYL)-2-PHENYLETHYL]-NALPHA-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE'>4KZ</scene>, <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=6wqh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wqh OCA], [https://pdbe.org/6wqh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wqh RCSB], [https://www.ebi.ac.uk/pdbsum/6wqh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wqh ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Lon AAA+ (adenosine triphosphatases associated with diverse cellular activities) protease (LonA) converts ATP-fuelled conformational changes into sufficient mechanical force to drive translocation of a substrate into a hexameric proteolytic chamber. To understand the structural basis for the substrate translocation process, we determined the cryo-electron microscopy (cryo-EM) structure of Meiothermus taiwanensis LonA (MtaLonA) in a substrate-engaged state at 3.6 A resolution. Our data indicate that substrate interactions are mediated by the dual pore loops of the ATPase domains, organized in spiral staircase arrangement from four consecutive protomers in different ATP-binding and hydrolysis states. However, a closed AAA+ ring is maintained by two disengaged ADP-bound protomers transiting between the lowest and highest position. This structure reveals a processive rotary translocation mechanism mediated by LonA-specific nucleotide-dependent allosteric coordination among the ATPase domains, which is induced by substrate binding.

Molecular basis for ATPase-powered substrate translocation by the Lon AAA+ protease.,Li S, Hsieh KY, Su SC, Pintilie GD, Zhang K, Chang CI J Biol Chem. 2021 Oct;297(4):101239. doi: 10.1016/j.jbc.2021.101239. Epub 2021 , Sep 24. PMID:34563541<ref>PMID:34563541</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6wqh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Dictyostelium discoideum]]
[[Category: Large Structures]]
[[Category: Meiothermus taiwanensis]]
[[Category: Chang C]]
[[Category: Chiu W]]
[[Category: Hsiehb K]]
[[Category: Li S]]
[[Category: Pintilie G]]
[[Category: Sub S]]
[[Category: Zhang K]]