3u2a

Adaptor dependent degradation of a cell-cycle regulator reveals diversity in substrate architectures

spinqualitylabelsall models 3u2a, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3u2a is a 1 chain structure with sequence from Caulobacter vibrioides. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: CSO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H3CDG5_CAUVN Publication Abstract from PubMed 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. Adaptor-dependent degradation of a cell-cycle regulator uses a unique substrate architecture.,Rood KL, Clark NE, Stoddard PR, Garman SC, Chien P Structure. 2012 Jul 3;20(7):1223-32. Epub 2012 Jun 7. PMID:22682744 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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