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6az0

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Mitochondrial ATPase Protease YME1

6az0, resolution 3.40Å

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Retrieved from "http://52.214.119.220/wiki/index.php/6az0"

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 ==Mitochondrial ATPase Protease YME1==
-<StructureSection load='6az0' size='340' side='right'caption='[[6az0]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
+<SX load='6az0' size='340' side='right' viewer='molstar' caption='[[6az0]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6az0]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AZ0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AZ0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6az0]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_RM11-1a Saccharomyces cerevisiae RM11-1a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AZ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AZ0 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 3.4&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SCRG_02514 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=285006 Baker's yeast])</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=6az0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6az0 OCA], [https://pdbe.org/6az0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6az0 RCSB], [https://www.ebi.ac.uk/pdbsum/6az0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6az0 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6az0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6az0 OCA], [http://pdbe.org/6az0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6az0 RCSB], [http://www.ebi.ac.uk/pdbsum/6az0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6az0 ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/B3LL85_YEAS1 B3LL85_YEAS1]
-We present an atomic model of a substrate-bound inner mitochondrial membrane AAA+ quality control protease in yeast, YME1. Our ~3.4-angstrom cryo-electron microscopy structure reveals how the adenosine triphosphatases (ATPases) form a closed spiral staircase encircling an unfolded substrate, directing it toward the flat, symmetric protease ring. Three coexisting nucleotide states allosterically induce distinct positioning of tyrosines in the central channel, resulting in substrate engagement and translocation to the negatively charged proteolytic chamber. This tight coordination by a network of conserved residues defines a sequential, around-the-ring adenosine triphosphate hydrolysis cycle that results in stepwise substrate translocation. A hingelike linker accommodates the large-scale nucleotide-driven motions of the ATPase spiral relative to the planar proteolytic base. The translocation mechanism is likely conserved for other AAA+ ATPases.
-Structure of the mitochondrial inner membrane AAA+ protease YME1 gives insight into substrate processing.,Puchades C, Rampello AJ, Shin M, Giuliano CJ, Wiseman RL, Glynn SE, Lander GC Science. 2017 Nov 3;358(6363). pii: eaao0464. doi: 10.1126/science.aao0464. PMID:29097521<ref>PMID:29097521</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 6az0" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
-</StructureSection>
+</SX>
-[[Category: Baker's yeast]]
 [[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Giuliano, C]]
+[[Category: Saccharomyces cerevisiae RM11-1a]]
-[[Category: Glynn, S E]]
+[[Category: Giuliano C]]
-[[Category: Lander, G C]]
+[[Category: Glynn SE]]
-[[Category: Puchades, C]]
+[[Category: Lander GC]]
-[[Category: Rampello, A J]]
+[[Category: Puchades C]]
-[[Category: Shin, M]]
+[[Category: Rampello AJ]]
-[[Category: Wiseman, R L]]
+[[Category: Shin M]]
-[[Category: Atpase]]
+[[Category: Wiseman RL]]
-[[Category: Hydrolase]]
-[[Category: Mitochondrial]]
-[[Category: Protease]]

6az0

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Mitochondrial ATPase Protease YME1

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