Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Catalytic cycling of human mitochondrial Lon protease.
Journal, issue, pages	Structure, Vol. 30, Issue 9, Page 1254-11268.e7, Year 2022
Publish date	Sep 1, 2022
Authors	Inayathulla Mohammed / Kai A Schmitz / Niko Schenck / Dimitrios Balasopoulos / Annika Topitsch / Timm Maier / Jan Pieter Abrahams /
PubMed Abstract	The mitochondrial Lon protease (LonP1) regulates mitochondrial health by removing redundant proteins from the mitochondrial matrix. We determined LonP1 in eight nucleotide-dependent conformational ...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.
External links	Structure / PubMed:35870450
Methods	EM (single particle)
Resolution	3.8 - 15.0 Å
Structure data	12306 7nfy EMDB-12306, PDB-7nfy: P1a-state of wild type human mitochondrial LONP1 protease with bound substrate protein and ATPgS Method: EM (single particle) / Resolution: 3.9 Å 12307 7ng4 EMDB-12307, PDB-7ng4: P1b-state of wild type human mitochondrial LONP1 protease with bound endogenous substrate protein and in presence of ATP/ADP mix Method: EM (single particle) / Resolution: 4.4 Å 12308 7ng5 EMDB-12308, PDB-7ng5: P1c-state of wild type human mitochondrial LONP1 protease with bound substrate protein in presence of ATP/ADP mix Method: EM (single particle) / Resolution: 3.8 Å 12312 7ngc EMDB-12312, PDB-7ngc: P2a-state of wild type human mitochondrial LONP1 protease with bound substrate protein and in presence of ATPgS Method: EM (single particle) / Resolution: 7.5 Å 12313 7ngf EMDB-12313, PDB-7ngf: P2c-state of wild type human mitochondrial LONP1 protease with bound endogenous substrate protein and in presence of ATP/ADP mix Method: EM (single particle) / Resolution: 5.6 Å 12315 7ngl EMDB-12315, PDB-7ngl: R-state of wild type human mitochondrial LONP1 protease bound to endogenous ADP Method: EM (single particle) / Resolution: 3.8 Å 12316 7ngp EMDB-12316, PDB-7ngp: D1-state of wild type human mitochondrial LONP1 protease Method: EM (single particle) / Resolution: 15.0 Å 12317 7ngq EMDB-12317, PDB-7ngq: Human mitochondrial Lon protease homolog, D2-state Method: EM (single particle) / Resolution: 12.0 Å 13102 7oxo EMDB-13102, PDB-7oxo: human LonP1, R-state, incubated in AMPPCP Method: EM (single particle) / Resolution: 3.9 Å
Chemicals	ChemComp-AGS: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogueYM ChemComp-MG: Unknown entry ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM / Adenosine diphosphate ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate
Source	homo sapiens (human)
Keywords	MOTOR PROTEIN / human mitochondrial AAA+ protease / protease / unfolds / hexamer / AAA+ protein / chaperone