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TitleProcessive cleavage of substrate at individual proteolytic active sites of the Lon protease complex.
Journal, issue, pagesSci Adv, Vol. 7, Issue 46, Page eabj9537, Year 2021
Publish dateNov 12, 2021
AuthorsShanshan Li / Kan-Yen Hsieh / Chiao-I Kuo / Shih-Chieh Su / Kai-Fa Huang / Kaiming Zhang / Chung-I Chang /
PubMed AbstractThe Lon protease is the prototype of a family of proteolytic machines with adenosine triphosphatase modules built into a substrate degradation chamber. Lon is known to degrade protein substrates in a ...The Lon protease is the prototype of a family of proteolytic machines with adenosine triphosphatase modules built into a substrate degradation chamber. Lon is known to degrade protein substrates in a processive fashion, cutting a protein chain processively into small peptides before commencing cleavages of another protein chain. Here, we present structural and biochemical evidence demonstrating that processive substrate degradation occurs at each of the six proteolytic active sites of Lon, which forms a deep groove that partially encloses the substrate polypeptide chain by accommodating only the unprimed residues and permits processive cleavage in the C-to-N direction. We identify a universally conserved acidic residue at the exit side of the binding groove indispensable for the proteolytic activity. This noncatalytic residue likely promotes processive proteolysis by carboxyl-carboxylate interactions with cleaved intermediates. Together, these results uncover a previously unrecognized mechanism for processive substrate degradation by the Lon protease.
External linksSci Adv / PubMed:34757797 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.1 - 3.28 Å
Structure data

EMDB-31589, PDB-7fid:
Processive cleavage of substrate at individual proteolytic active sites of the Lon proteasecomplex (conformation 1)
Method: EM (single particle) / Resolution: 2.44 Å

EMDB-31590, PDB-7fie:
Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex (conformation 2)
Method: EM (single particle) / Resolution: 2.36 Å

EMDB-31607, PDB-7fiz:
Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex (conformation 3)
Method: EM (single particle) / Resolution: 3.28 Å

PDB-7eux:
Crystal structure of the Lon-like protease MtaLonC with D581A mutation in complex with substrate polypeptide
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

PDB-7euy:
Crystal structure of the Lon-like protease MtaLonC with D582A mutation in complex with substrate polypeptide
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-7ev4:
Crystal structure of the Lon-like protease MtaLonC with S582A mutation in complex with F-b20-Q
Method: X-RAY DIFFRACTION / Resolution: 2.12 Å

PDB-7ev6:
Crystal structure of the Lon-like protease MtaLonC with D581A mutation in complex with F-b20-Q
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION / Phosphate

ChemComp-HOH:
WATER / Water

ChemComp-AGS:
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

Source
  • meiothermus taiwanensis wr-220 (bacteria)
  • meiothermus taiwanensis (bacteria)
  • escherichia coli (E. coli)
KeywordsHYDROLASE / protease / TTC1975 peptidase / Lon-like protease / AAA / complex / proteolysis

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