7ngc
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==P2a-state of wild type human mitochondrial LONP1 protease with bound substrate protein and in presence of ATPgS== |
| - | <StructureSection load='7ngc' size='340' side='right'caption='[[7ngc]]' scene=''> | + | <StructureSection load='7ngc' size='340' side='right'caption='[[7ngc]], [[Resolution|resolution]] 7.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7ngc]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NGC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NGC FirstGlance]. <br> |
| - | </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=7ngc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ngc OCA], [https://pdbe.org/7ngc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ngc RCSB], [https://www.ebi.ac.uk/pdbsum/7ngc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ngc ProSAT]</span></td></tr> | + | </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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7ngc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ngc OCA], [https://pdbe.org/7ngc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ngc RCSB], [https://www.ebi.ac.uk/pdbsum/7ngc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ngc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/LONM_HUMAN LONM_HUMAN] ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial promoters and RNA in a single-stranded, site-specific, and strand-specific manner. May regulate mitochondrial DNA replication and/or gene expression using site-specific, single-stranded DNA binding to target the degradation of regulatory proteins binding to adjacent sites in mitochondrial promoters. Endogenous substrates include mitochondrial steroidogenic acute regulatory (StAR) protein.[HAMAP-Rule:MF_03120]<ref>PMID:12198491</ref> <ref>PMID:15870080</ref> <ref>PMID:17420247</ref> <ref>PMID:8248235</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The mitochondrial Lon protease (LonP1) regulates mitochondrial health by removing redundant proteins from the mitochondrial matrix. We determined LonP1 in eight nucleotide-dependent conformational states by cryoelectron microscopy (cryo-EM). The flexible assembly of N-terminal domains had 3-fold symmetry, and its orientation depended on the conformational state. We show that a conserved structural motif around T803 with a high similarity to the trypsin catalytic triad is essential for proteolysis. We show that LonP1 is not regulated by redox potential, despite the presence of two conserved cysteines at disulfide-bonding distance in its unfoldase core. Our data indicate how sequential ATP hydrolysis controls substrate protein translocation in a 6-fold binding change mechanism. Substrate protein translocation, rather than ATP hydrolysis, is a rate-limiting step, suggesting that LonP1 is a Brownian ratchet with ATP hydrolysis preventing translocation reversal. 3-fold rocking motions of the flexible N-domain assembly may assist thermal unfolding of the substrate protein. | ||
| + | |||
| + | Catalytic cycling of human mitochondrial Lon protease.,Mohammed I, Schmitz KA, Schenck N, Balasopoulos D, Topitsch A, Maier T, Abrahams JP Structure. 2022 Jul 12. pii: S0969-2126(22)00269-6. doi:, 10.1016/j.str.2022.06.006. PMID:35870450<ref>PMID:35870450</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7ngc" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Abrahams JP]] |
| + | [[Category: Maier T]] | ||
| + | [[Category: Mohammed I]] | ||
| + | [[Category: Schenck N]] | ||
| + | [[Category: Schmitz KA]] | ||
Revision as of 07:43, 9 November 2022
P2a-state of wild type human mitochondrial LONP1 protease with bound substrate protein and in presence of ATPgS
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