3U2A
Adaptor dependent degradation of a cell-cycle regulator reveals diversity in substrate architectures
Summary for 3U2A
| Entry DOI | 10.2210/pdb3u2a/pdb |
| Descriptor | GGDEF family protein (2 entities in total) |
| Functional Keywords | phosphodiesterase, proteolysis, cell-cycle, clpxp, cyclic di-gmp, hydrolase |
| Biological source | Caulobacter vibrioides |
| Total number of polymer chains | 1 |
| Total formula weight | 13978.76 |
| Authors | Rood, K.,Clark, N.E.,Garman, S.C.,Chien, P. (deposition date: 2011-10-02, release date: 2012-05-30, Last modification date: 2024-11-06) |
| Primary citation | Rood, K.L.,Clark, N.E.,Stoddard, P.R.,Garman, S.C.,Chien, P. Adaptor-dependent degradation of a cell-cycle regulator uses a unique substrate architecture. Structure, 20:1223-1232, 2012 Cited by PubMed Abstract: In Caulobacter crescentus, the ClpXP protease degrades several crucial cell-cycle regulators, including the phosphodiesterase PdeA. Degradation of PdeA requires the response regulator CpdR and signals a morphological transition in concert with initiation of DNA replication. Here, we report the structure of a Per-Arnt-Sim (PAS) domain of PdeA and show that it is necessary for CpdR-dependent degradation in vivo and in vitro. CpdR acts as an adaptor, tethering the amino-terminal PAS domain to ClpXP and promoting recognition of the weak carboxyl-terminal degron of PdeA, a combination that ensures processive proteolysis. We identify sites on the PAS domain needed for CpdR recognition and find that one subunit of the PdeA dimer can be delivered to ClpXP by its partner. Finally, we show that improper stabilization of PdeA in vivo alters cellular behavior. These results introduce an adaptor/substrate pair for ClpXP and reveal broad diversity in adaptor-mediated proteolysis. PubMed: 22682744DOI: 10.1016/j.str.2012.04.019 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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