User:Tilman Schirmer/Sandbox 213
From Proteopedia
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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. | 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. | ||
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| + | ==References== | ||
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| + | Activated PleD structure [[2v0n]]: | ||
| + | <ref group="xtra">PMID:17697997</ref> | ||
| + | <references group="xtra"/> | ||
Revision as of 08:47, 15 July 2009
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
