2v0n

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

Structural highlights

2v0n is a 2 chain structure with sequence from Caulobacter vibrioides CB15. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.71Å
Ligands:BEF, C2E, CL, GAV, MG, SO4
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PLED_CAUVN Response regulator that is part of a signal transduction pathway controlling cell differentiation in the swarmer-to-stalked cell transition.[1] Catalyzes the condensation of two GTP molecules to the cyclic dinucleotide di-GMP (c-di-GMP), which acts as a secondary messenger.[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

Structure of BeF3- -modified response regulator PleD: implications for diguanylate cyclase activation, catalysis, and feedback inhibition.,Wassmann P, Chan C, Paul R, Beck A, Heerklotz H, Jenal U, Schirmer T Structure. 2007 Aug;15(8):915-27. PMID:17697997[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
24 reviews cite this structure
Principles of c-di-GMP signalling in bacteria.
Hengge et al. (2009)
23 more
95 other articles
No citations found

See Also

References

  1. ↑ Aldridge P, Paul R, Goymer P, Rainey P, Jenal U. Role of the GGDEF regulator PleD in polar development of Caulobacter crescentus. Mol Microbiol. 2003 Mar;47(6):1695-708. PMID:12622822 doi:10.1046/j.1365-2958.2003.03401.x
  2. ↑ Paul R, Weiser S, Amiot NC, Chan C, Schirmer T, Giese B, Jenal U. Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain. Genes Dev. 2004 Mar 15;18(6):715-27. PMID:15075296 doi:http://dx.doi.org/10.1101/gad.289504
  3. ↑ 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

Contents


PDB ID 2v0n

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