7ev6 | pdb_00007ev6

Crystal structure of the Lon-like protease MtaLonC with D581A mutation in complex with F-b20-Q

spinqualitylabelsall models 7ev6, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7ev6 is a 2 chain structure with sequence from Escherichia coli and Meiothermus taiwanensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: NIY, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C9DRU9_9DEIN Publication Abstract from PubMed 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. Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex.,Li S, Hsieh KY, Kuo CI, Su SC, Huang KF, Zhang K, Chang CI Sci Adv. 2021 Nov 12;7(46):eabj9537. doi: 10.1126/sciadv.abj9537. Epub 2021 Nov , 10. PMID:34757797 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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