7EV4
Crystal structure of the Lon-like protease MtaLonC with S582A mutation in complex with F-b20-Q
Summary for 7EV4
| Entry DOI | 10.2210/pdb7ev4/pdb |
| Descriptor | Endopeptidase La, F-b20-Q peptide {ortho-aminobenzoic acid (Abz)- QLRSLNGEWRFAWFPAPEAV[Tyr(3-NO2)]A}, PHOSPHATE ION, ... (4 entities in total) |
| Functional Keywords | hydrolase, protease, ttc1975 peptidase, lon-like protease |
| Biological source | Meiothermus taiwanensis More |
| Total number of polymer chains | 2 |
| Total formula weight | 81104.79 |
| Authors | Hsieh, K.Y.,Kuo, C.I.,Su, S.C.,Huang, K.F.,Chang, C.I. (deposition date: 2021-05-20, release date: 2021-11-24, Last modification date: 2023-11-29) |
| Primary citation | Li, S.,Hsieh, K.Y.,Kuo, C.I.,Su, S.C.,Huang, K.F.,Zhang, K.,Chang, C.I. Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex. Sci Adv, 7:eabj9537-eabj9537, 2021 Cited by PubMed Abstract: 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. PubMed: 34757797DOI: 10.1126/sciadv.abj9537 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.12 Å) |
Structure validation
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