Sandbox Reserved 1644: Difference between revisions
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== General structure == | == General structure == | ||
Lon proteins are grouped into two families, '''LonA''' and '''LonB'''. The human protein LonP1 is part of the LonA proteins. This protein has three isoforms obtained by [https://en.wikipedia.org/wiki/Alternative_splicing alternative splicing] of the portion of DNA coding for this protein. | |||
Globally there is a great diversity of Lon proteins, but they are all organised in an oligomeric ring structure, mostly hexameric structure with identical subunits. | Globally there is a great diversity of Lon proteins, but they are all organised in an oligomeric ring structure, mostly hexameric structure with identical subunits. | ||
Lon proteins are therefore an hexameric chambered [https://en.wikipedia.org/wiki/Protease protease] complex. (This structure is similar with yeast [https://www.yeastgenome.org/locus/S000000118 Pim1] ) | Lon proteins are therefore an hexameric chambered [https://en.wikipedia.org/wiki/Protease protease] complex. (This structure is similar with yeast [https://www.yeastgenome.org/locus/S000000118 Pim1] ) | ||
The six Lon monomers are forming three pairs of legs owned by the N-terminal domain of the protein. This structure is emerging of the protein as a trimer of dimers. | The six Lon monomers are forming three pairs of legs owned by the N-terminal domain of the protein. This structure is emerging of the protein as a trimer of dimers. | ||
Like many proteins, Lon is a '''flexible''' peptide which has different '''three-dimensional conformations'''. The protein can therefore pass from one conformation to another by hydrolysis of [https://biologydictionary.net/atp/ ATP]. | Like many proteins, Lon is a '''flexible''' peptide which has different '''three-dimensional conformations'''. The protein can therefore pass from one conformation to another by hydrolysis of [https://biologydictionary.net/atp/ ATP]. | ||
