4AG0
Crystal structure of FimX EAL domain
Summary for 4AG0
| Entry DOI | 10.2210/pdb4ag0/pdb |
| Related | 4AFY |
| Descriptor | FIMX, PHOSPHATE ION, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | hydrolase, phosphodiesterase, c-digmp, biofilm |
| Biological source | PSEUDOMONAS AERUGINOSA |
| Total number of polymer chains | 2 |
| Total formula weight | 60908.74 |
| Authors | Robert-Paganin, J.,Nonin-Lecomte, S.,Rety, S. (deposition date: 2012-01-23, release date: 2013-01-09, Last modification date: 2023-12-20) |
| Primary citation | Robert-Paganin, J.,Nonin-Lecomte, S.,Rety, S. Crystal Structure of an Eal Domain in Complex with Reaction Product 5'-Pgpg Plos One, 7:52424-, 2012 Cited by PubMed 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. PubMed: 23285035DOI: 10.1371/JOURNAL.PONE.0052424 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.304 Å) |
Structure validation
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