User:Tilman Schirmer/Sandbox 213
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< User:Tilman Schirmer(Difference between revisions)
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<applet load='2v0n' scene='User:Tilman_Schirmer/Sandbox_213/Tight_dimer/2' size='400' frame='true' align='right' caption='activated (BeF3- modified; [[2v0n]]' /> | <applet load='2v0n' scene='User:Tilman_Schirmer/Sandbox_213/Tight_dimer/2' size='400' frame='true' align='right' caption='activated (BeF3- modified; [[2v0n]]' /> | ||
| - | PleD shows direct non-competitive feedback inibition with a K<sub>i</sub> of about 1 μM. There are two allosteric sites, the <scene name='User:Tilman_Schirmer/Sandbox_213/Ip/ | + | PleD shows direct non-competitive feedback inibition with a K<sub>i</sub> of about 1 μM. There are two allosteric sites, the <scene name='User:Tilman_Schirmer/Sandbox_213/Ip/4'>''primary'' inhibition site</scene> I<sub>p</sub> (R<sub>359</sub> and D<sub>362</sub> of a RxxD sequence motif and R<sub>390</sub>), and the <scene name='User:Tilman_Schirmer/Sandbox_213/Is/3'>"secondary'' inhibition site</scene> I<sub>s</sub> (R<sub>313</sub>) in the PleD GGDEF domain that are involved in product binding across to GGDEF domains (cross-linking). <br><br> |
Binding of two intercalated <scene name='User:Tilman_Schirmer/Sandbox_213/C-di-gmp_dimer/1'>(c-di-GMP)2 dimers</scene> results in <scene name='User:Tilman_Schirmer/Sandbox_213/Complex/6'>cross-linking</scene> of the two GGDEF domains in the dimer and keeps the two active sites (with bound <scene name='User:Tilman_Schirmer/Sandbox_213/Complex/8'>substrate analog</scene>) apart form each other. <br><br><br><br> | Binding of two intercalated <scene name='User:Tilman_Schirmer/Sandbox_213/C-di-gmp_dimer/1'>(c-di-GMP)2 dimers</scene> results in <scene name='User:Tilman_Schirmer/Sandbox_213/Complex/6'>cross-linking</scene> of the two GGDEF domains in the dimer and keeps the two active sites (with bound <scene name='User:Tilman_Schirmer/Sandbox_213/Complex/8'>substrate analog</scene>) apart form each other. <br><br><br><br> | ||
Current revision
PleD allosteric product inhibition
Allosteric product inhibition
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PleD shows direct non-competitive feedback inibition with a Ki of about 1 μM. There are two allosteric sites, the Ip (R359 and D362 of a RxxD sequence motif and R390), and the Is (R313) in the PleD GGDEF domain that are involved in product binding across to GGDEF domains (cross-linking).
Binding of two intercalated results in of the two GGDEF domains in the dimer and keeps the two active sites (with bound ) apart form each other.
References
Activated PleD structure 2v0n:
- Wassmann P, Chan C, Paul R, Beck A, Heerklotz H, Jenal U, Schirmer T. Structure of BeF3- -modified response regulator PleD: implications for diguanylate cyclase activation, catalysis, and feedback inhibition. Structure. 2007 Aug;15(8):915-27. PMID:17697997 doi:http://dx.doi.org/10.1016/j.str.2007.06.016
