6on2: Difference between revisions

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 <SX load='6on2' size='340' side='right' viewer='molstar' caption='[[6on2]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6on2]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pestis"_(lehmann_and_neumann_1896)_migula_1900 "bacillus pestis" (lehmann and neumann 1896) migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ON2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ON2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6on2]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ON2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ON2 FirstGlance]. <br>
-</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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lon, YP_0776, EGT45_05820, NCTC144_01047 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=632 "Bacillus pestis" (Lehmann and Neumann 1896) Migula 1900])</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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] </span></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=6on2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6on2 OCA], [https://pdbe.org/6on2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6on2 RCSB], [https://www.ebi.ac.uk/pdbsum/6on2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6on2 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6on2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6on2 OCA], [http://pdbe.org/6on2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6on2 RCSB], [http://www.ebi.ac.uk/pdbsum/6on2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6on2 ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/A0A5P8YJ65_YERPE A0A5P8YJ65_YERPE] ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.[HAMAP-Rule:MF_01973]
-Substrate-bound structures of AAA+ protein translocases reveal a conserved asymmetric spiral staircase architecture wherein a sequential ATP hydrolysis cycle drives hand-over-hand substrate translocation. However, this configuration is unlikely to represent the full conformational landscape of these enzymes, as biochemical studies suggest distinct conformational states depending on the presence or absence of substrate. Here, we used cryo-electron microscopy to determine structures of the Yersinia pestis Lon AAA+ protease in the absence and presence of substrate, uncovering the mechanistic basis for two distinct operational modes. In the absence of substrate, Lon adopts a left-handed, "open" spiral organization with autoinhibited proteolytic active sites. Upon the addition of substrate, Lon undergoes a reorganization to assemble an enzymatically active, right-handed "closed" conformer with active protease sites. These findings define the mechanistic principles underlying the operational plasticity required for processing diverse protein substrates.
-Structural basis for distinct operational modes and protease activation in AAA+ protease Lon.,Shin M, Puchades C, Asmita A, Puri N, Adjei E, Wiseman RL, Karzai AW, Lander GC Sci Adv. 2020 May 20;6(21):eaba8404. doi: 10.1126/sciadv.aba8404. eCollection, 2020 May. PMID:32490208<ref>PMID:32490208</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 6on2" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </SX>
-[[Category: Endopeptidase La]]
 [[Category: Large Structures]]
-[[Category: Adjei, E]]
+[[Category: Yersinia pestis]]
-[[Category: Asmita, A]]
+[[Category: Adjei E]]
-[[Category: Karzai, A W]]
+[[Category: Asmita A]]
-[[Category: Lander, G C]]
+[[Category: Karzai AW]]
-[[Category: Puchades, C]]
+[[Category: Lander GC]]
-[[Category: Shin, M]]
+[[Category: Puchades C]]
-[[Category: Wiseman, R L]]
+[[Category: Shin M]]
-[[Category: Aaa+]]
+[[Category: Wiseman RL]]
-[[Category: Atpase]]
-[[Category: Hydrolase]]
-[[Category: Lon]]
-[[Category: Mitochondrial protease]]