Sandbox Reserved 1644: Difference between revisions

Line 43:

. The protein can therefore pass from one conformation to another by hydrolysis of [https://biologydictionary.net/atp/ ATP]<ref>Voos, Wolfgang, et Karen Pollecker. « The Mitochondrial Lon Protease: Novel Functions off the Beaten Track? » Biomolecules 10, nᵒ 2 (7 février 2020). https://doi.org/10.3390/biom10020253.

</ref>.

In the substrate-engaged form, sequential ATP hydrolysis drives the progressive translocation of unfolded substrates from the AAA+ channel towards the protease domains. With these conformational changes, the [https://en.wikipedia.org/wiki/Active_site '''active sites'''] of the Lon protein are protected from the external environment in the oligomeric complex that forms the '''degradation chamber'''.

In the substrate-engaged form, sequential ATP hydrolysis drives the progressive translocation of unfolded substrates from the AAA+ channel towards the protease domains. With these conformational changes, the [https://en.wikipedia.org/wiki/Active_site '''active sites'''] of the Lon protein are protected from the external environment in the oligomeric complex that forms the '''degradation chamber'''. This mechanism is likely to be conserved in all Lon proteases and is related to the rotary treadmilling mechanism of other AAA+ translocases. The N-terminal domains show much larger sequence divergences across species and kingdoms than the A and P domains, and this is possibly related to organism-specific substrate recognition requirements. <ref>Coscia, F., & Löwe, J. (2021). Cryo‐EM structure of the full‐length Lon protease from Thermus thermophilus. FEBS letters, 595(21), 2691-2700.</ref>

This form of degradation chamber is also found in bacteria, plants, fungi and metazoan, the similarities with bacteria are most probably due to the [https://en.wikipedia.org/wiki/Symbiogenesis endosymbiotic theory].

<br>

Sandbox Reserved 1644: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 43: / Line 43: @@
 .  The protein can therefore pass from one conformation to another by hydrolysis of [https://biologydictionary.net/atp/ ATP]<ref>Voos, Wolfgang, et Karen Pollecker. « The Mitochondrial Lon Protease: Novel Functions off the Beaten Track? » Biomolecules 10, nᵒ 2 (7 février 2020). https://doi.org/10.3390/biom10020253.
 </ref>.
-In the substrate-engaged form, sequential ATP hydrolysis drives the progressive translocation of unfolded substrates from the AAA+ channel towards the protease domains. With these conformational changes, the [https://en.wikipedia.org/wiki/Active_site '''active sites'''] of the Lon protein are protected from the external environment in the oligomeric complex that forms the '''degradation chamber'''.
+In the substrate-engaged form, sequential ATP hydrolysis drives the progressive translocation of unfolded substrates from the AAA+ channel towards the protease domains. With these conformational changes, the [https://en.wikipedia.org/wiki/Active_site '''active sites'''] of the Lon protein are protected from the external environment in the oligomeric complex that forms the '''degradation chamber'''. This mechanism is likely to be conserved in all Lon proteases and is related to the rotary treadmilling mechanism of other AAA+ translocases. The N-terminal domains show much larger sequence divergences across species and kingdoms than the A and P domains, and this is possibly related to organism-specific substrate recognition requirements. <ref>Coscia, F., & Löwe, J. (2021). Cryo‐EM structure of the full‐length Lon protease from Thermus thermophilus. FEBS letters, 595(21), 2691-2700.</ref>
 This form of degradation chamber is also found in bacteria, plants, fungi and metazoan, the similarities with bacteria are most probably due to the [https://en.wikipedia.org/wiki/Symbiogenesis endosymbiotic theory].
 <br>