Sandbox Reserved 1644: Difference between revisions
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This protein has a [https://en.wikipedia.org/wiki/Proteolysis '''proteolytic'''] and [https://en.wikipedia.org/wiki/Chaperone_(protein) '''chaperone''']-like activity, it cannot unfold aggregated proteins, but can participate in the assembling of some complexes). These two enzymatic activities are separated on two polypeptide chains forming a complex or two separate domains on the same polypeptide chain. | This protein has a [https://en.wikipedia.org/wiki/Proteolysis '''proteolytic'''] and [https://en.wikipedia.org/wiki/Chaperone_(protein) '''chaperone''']-like activity, it cannot unfold aggregated proteins, but can participate in the assembling of some complexes). These two enzymatic activities are separated on two polypeptide chains forming a complex or two separate domains on the same polypeptide chain. | ||
The Lon protein has three main distinct domains: the first, the '''N-terminal''' domain, is specialised in '''substrate binding''' and [https://en.wikipedia.org/wiki/Oligomer '''oligomerization''']. The second, called the '''AAA+ domain''' (or A domain) corresponds to the fixation and hydrolysis site of the [https://biologydictionary.net/atp/ATP]. Finally, the third domain located at the '''C-terminal''' is an active serine site leading to '''substrate degradation'''. This is a [https://en.wikipedia.org/wiki/Proteolysis '''proteolytic'''] domain, called domain P. | |||
