2V0N

ACTIVATED RESPONSE REGULATOR PLED IN COMPLEX WITH C-DIGMP AND GTP- ALPHA-S

Summary for 2V0N

• Entry DOI: 10.2210/pdb2v0n/pdb
• Related: 1W25 2WB4
• Descriptor: RESPONSE REGULATOR PLED, BERYLLIUM TRIFLUORIDE ION, MAGNESIUM ION, ... (8 entities in total)
• Functional Keywords: beryllium fluoride modification, allosteric product inhibition, response regulator, lyase, cell cycle, transducer, magnesium, two-component system
• Biological source: CAULOBACTER VIBRIOIDES
• Total number of polymer chains: 2
• Total formula weight: 105098.38

Authors

Wassmann, P.,Schirmer, T. (deposition date: 2007-05-15, release date: 2007-08-21, Last modification date: 2023-12-13)

Primary citation

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, 15:915-, 2007

PubMed Abstract: Cyclic di-guanosine monophosphate (c-di-GMP) is a ubiquitous bacterial second messenger involved in the regulation of cell surface-associated traits and persistence. We have determined the crystal structure of PleD from Caulobacter crescentus, a response regulator with a diguanylate cyclase (DGC) domain, in its activated form. The BeF(3)(-) modification of its receiver domain causes rearrangement with respect to an adaptor domain, which, in turn, promotes dimer formation, allowing for the efficient encounter of two symmetric catalytic domains. The substrate analog GTPalphaS and two putative cations are bound to the active sites in a manner similar to adenylate cyclases, suggesting an analogous two-metal catalytic mechanism. An allosteric c-di-GMP-binding mode that crosslinks DGC and an adaptor domain had been identified before. Here, a second mode is observed that crosslinks the DGC domains within a PleD dimer. Both modes cause noncompetitive product inhibition by domain immobilization.

PubMed: 17697997
DOI: 10.1016/J.STR.2007.06.016

Experimental method

X-RAY DIFFRACTION (2.71 Å)