4afy › Citations

Crystal structure of an EAL domain in complex with reaction product 5'-pGpG.

<div class='caption-title'>Structure of the homodimer of EAL domain of FimX with bound 5′-pGpG.</div>
<div class='caption-title'>Stereo view of the active site of FimX-EAL domain.</div>
<div class='caption-title'>Representation of the cavity in the dimer of FimX-EAL bound to pGpG.</div>
Robert-Paganin J, Nonin-Lecomte S, Réty S
OpenAccess logo PLoS One 7 e52424 (2012)
Cited: 10 times
EuropePMC logo PMID: 23285035

Abstract

FimX is a large multidomain protein containing an EAL domain and involved in twitching motility in Pseudomonas aeruginosa. We present here two crystallographic structures of the EAL domain of FimX (residues 438-686): one of the apo form and the other of a complex with 5'-pGpG, the reaction product of the hydrolysis of c-di-GMP. In both crystal forms, the EAL domains form a dimer delimiting a large cavity encompassing the catalytic pockets. The ligand is trapped in this cavity by its sugar phosphate moiety. We confirmed by NMR that the guanine bases are not involved in the interaction in solution. We solved here the first structure of an EAL domain bound to the reaction product 5'-pGpG. Though isolated FimX EAL domain has a very low catalytic activity, which would not be significant compared to other catalytic EAL domains, the structure with the product of the reaction can provides some hints in the mechanism of hydrolysis of the c-di-GMP by EAL domains.

Articles - 4afy mentioned but not cited (2)

  1. Dimerisation induced formation of the active site and the identification of three metal sites in EAL-phosphodiesterases. Bellini D, Horrell S, Hutchin A, Phippen CW, Strange RW, Cai Y, Wagner A, Webb JS, Tews I, Walsh MA. Sci Rep 7 42166 (2017)
  2. Crystal structure of an EAL domain in complex with reaction product 5'-pGpG. Robert-Paganin J, Nonin-Lecomte S, Réty S. PLoS One 7 e52424 (2012)


Articles citing this publication (8)

  1. Oligoribonuclease is the primary degradative enzyme for pGpG in Pseudomonas aeruginosa that is required for cyclic-di-GMP turnover. Orr MW, Donaldson GP, Severin GB, Wang J, Sintim HO, Waters CM, Lee VT. Proc Natl Acad Sci U S A 112 E5048-57 (2015)
  2. Inherent regulation of EAL domain-catalyzed hydrolysis of second messenger cyclic di-GMP. Sundriyal A, Massa C, Samoray D, Zehender F, Sharpe T, Jenal U, Schirmer T. J Biol Chem 289 6978-6990 (2014)
  3. Interaction of the cyclic-di-GMP binding protein FimX and the Type 4 pilus assembly ATPase promotes pilus assembly. Jain R, Sliusarenko O, Kazmierczak BI. PLoS Pathog 13 e1006594 (2017)
  4. Local c-di-GMP Signaling in the Control of Synthesis of the E. coli Biofilm Exopolysaccharide pEtN-Cellulose. Richter AM, Possling A, Malysheva N, Yousef KP, Herbst S, von Kleist M, Hengge R. J Mol Biol 432 4576-4595 (2020)
  5. Transmembrane redox control and proteolysis of PdeC, a novel type of c-di-GMP phosphodiesterase. Herbst S, Lorkowski M, Sarenko O, Nguyen TKL, Jaenicke T, Hengge R. EMBO J 37 e97825 (2018)
  6. Differential impact on motility and biofilm dispersal of closely related phosphodiesterases in Pseudomonas aeruginosa. Cai YM, Hutchin A, Craddock J, Walsh MA, Webb JS, Tews I. Sci Rep 10 6232 (2020)
  7. Regulation of Exopolysaccharide Production by ProE, a Cyclic-Di-GMP Phosphodiesterase in Pseudomonas aeruginosa PAO1. Feng Q, Ahator SD, Zhou T, Liu Z, Lin Q, Liu Y, Huang J, Zhou J, Zhang LH. Front Microbiol 11 1226 (2020)
  8. Analysis of proton wires in the enzyme active site suggests a mechanism of c-di-GMP hydrolysis by the EAL domain phosphodiesterases. Grigorenko BL, Knyazeva MA, Nemukhin AV. Proteins 84 1670-1680 (2016)


Quick links