|Entry||Database: PDB / ID: 7fd4|
|Title||A complete three-dimensional structure of the Lon protease translocating a protein substrate (conformation 1)|
|Keywords||HYDROLASE/PROTEIN BINDING / AAA+ protease / Lon / complete three-dimensional structure / N-terminal domain / CYTOSOLIC PROTEIN / HYDROLASE-PROTEIN BINDING complex|
|Function / homology|
Function and homology information
endopeptidase La / protein quality control for misfolded or incompletely synthesized proteins / ATP-dependent peptidase activity / cellular response to heat / sequence-specific DNA binding / serine-type endopeptidase activity / ATP binding / identical protein binding / cytoplasm
Similarity search - Function
Lon protease, bacterial / Peptidase S16, active site / Lon protease, bacterial/eukaryotic-type / ATP-dependent serine proteases, lon family, serine active site. / Lon protease (S16) C-terminal proteolytic domain / Lon protease / Peptidase S16, Lon proteolytic domain / Lon proteolytic domain profile. / Lon N-terminal domain profile. / Found in ATP-dependent protease La (LON) ...Lon protease, bacterial / Peptidase S16, active site / Lon protease, bacterial/eukaryotic-type / ATP-dependent serine proteases, lon family, serine active site. / Lon protease (S16) C-terminal proteolytic domain / Lon protease / Peptidase S16, Lon proteolytic domain / Lon proteolytic domain profile. / Lon N-terminal domain profile. / Found in ATP-dependent protease La (LON) / Lon, substrate-binding domain / ATP-dependent protease La (LON) substrate-binding domain / PUA-like superfamily / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core / Ribosomal protein S5 domain 2-type fold, subgroup / Ribosomal protein S5 domain 2-type fold / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Chem-4KZ / ADENOSINE-5'-DIPHOSPHATE / PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / Lon protease
Similarity search - Component
|Biological species||Meiothermus taiwanensis (bacteria)|
Bos taurus (cattle)
|Method||ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.4 Å|
|Authors||Li, S. / Hsieh, K. / Kuo, C. / Lee, S. / Pintilie, G. / Zhang, K. / Chang, C.|
|Funding support|| Taiwan, 1items |
|Citation||Journal: Sci Adv / Year: 2021|
Title: Complete three-dimensional structures of the Lon protease translocating a protein substrate.
Authors: Shanshan Li / Kan-Yen Hsieh / Chiao-I Kuo / Szu-Hui Lee / Grigore D Pintilie / Kaiming Zhang / Chung-I Chang /
Abstract: [Figure: see text].
|Structure viewer||Molecule: |
Downloads & links
B: Lon protease
C: Lon protease
D: Lon protease
E: Lon protease
F: Lon protease
A: Lon protease
Mass: 88554.594 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Meiothermus taiwanensis (bacteria) / Gene: lonA1, lon / Production host: Escherichia coli (E. coli) / References: UniProt: A0A059VAZ3, endopeptidase La
Mass: 1890.321 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle)
Mass: 523.247 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C10H16N5O12P3S / Feature type: SUBJECT OF INVESTIGATION / Comment: ATP-gamma-S, energy-carrying molecule analogue*YM
Mass: 418.253 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C22H23BN4O4 / Feature type: SUBJECT OF INVESTIGATION
Mass: 427.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Feature type: SUBJECT OF INVESTIGATION / Comment: ADP, energy-carrying molecule*YM
|Has ligand of interest||Y||Sequence details||Authors know the sequence of chain S (UNP P02662) but don't know how the coordinates align with the ...Authors know the sequence of chain S (UNP P02662) but don't know how the coordinates align with the sequence. P02662 sequence is MKLLILTCLV|
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction|
|Molecular weight||Value: 0.37 MDa / Experimental value: YES|
|Source (recombinant)||Organism: Escherichia coli (E. coli)|
|Buffer solution||pH: 8|
|Specimen||Conc.: 0.5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Microscopy||Model: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM|
|Electron lens||Mode: BRIGHT FIELDBright-field microscopy|
|Image recording||Electron dose: 48 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k)|
|CTF correction||Type: NONE|
|Symmetry||Point symmetry: C1 (asymmetric)|
|3D reconstruction||Resolution: 2.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 158553 / Symmetry type: POINT|
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